Comparison of initiation of protein synthesis in procaryotes, eucaryotes, and organelles (original) (raw)

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Selected References

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  1. Adams J. M., Capecchi M. R. N-formylmethionyl-sRNA as the initiator of protein synthesis. Proc Natl Acad Sci U S A. 1966 Jan;55(1):147–155. doi: 10.1073/pnas.55.1.147. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Adhya S., Gottesman M. Control of transcription termination. Annu Rev Biochem. 1978;47:967–996. doi: 10.1146/annurev.bi.47.070178.004535. [DOI] [PubMed] [Google Scholar]
  3. Ahlquist P., Dasgupta R., Shih D. S., Zimmern D., Kaesberg P. Two-step binding of eukaryotic ribosomes to brome mosaic virus RNA3. Nature. 1979 Sep 27;281(5729):277–282. doi: 10.1038/281277a0. [DOI] [PubMed] [Google Scholar]
  4. Akusjärvi G., Persson H. Controls of RNA splicing and termination in the major late adenovirus transcription unit. Nature. 1981 Jul 30;292(5822):420–426. doi: 10.1038/292420a0. [DOI] [PubMed] [Google Scholar]
  5. Alton N. K., Buxton F., Patel V., Giles N. H., Vapnek D. 5'-Untranslated sequences of two structural genes in the qa gene cluster of Neurospora crassa. Proc Natl Acad Sci U S A. 1982 Mar;79(6):1955–1959. doi: 10.1073/pnas.79.6.1955. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Amara S. G., Jonas V., Rosenfeld M. G., Ong E. S., Evans R. M. Alternative RNA processing in calcitonin gene expression generates mRNAs encoding different polypeptide products. Nature. 1982 Jul 15;298(5871):240–244. doi: 10.1038/298240a0. [DOI] [PubMed] [Google Scholar]
  7. Ambros V., Pettersson R. F., Baltimore D. An enzymatic activity in uninfected cells that cleaves the linkage between poliovirion RNA and the 5' terminal protein. Cell. 1978 Dec;15(4):1439–1446. doi: 10.1016/0092-8674(78)90067-3. [DOI] [PubMed] [Google Scholar]
  8. Amils R., Matthews E. A., Cantor C. R. An efficient in vitro total reconstitution of the Escherichia coli 50S ribosomal subunit. Nucleic Acids Res. 1978 Jul;5(7):2455–2470. doi: 10.1093/nar/5.7.2455. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Anderson S., Bankier A. T., Barrell B. G., de Bruijn M. H., Coulson A. R., Drouin J., Eperon I. C., Nierlich D. P., Roe B. A., Sanger F. Sequence and organization of the human mitochondrial genome. Nature. 1981 Apr 9;290(5806):457–465. doi: 10.1038/290457a0. [DOI] [PubMed] [Google Scholar]
  10. Anderson S., de Bruijn M. H., Coulson A. R., Eperon I. C., Sanger F., Young I. G. Complete sequence of bovine mitochondrial DNA. Conserved features of the mammalian mitochondrial genome. J Mol Biol. 1982 Apr 25;156(4):683–717. doi: 10.1016/0022-2836(82)90137-1. [DOI] [PubMed] [Google Scholar]
  11. Atkins J. F. Is UAA or UGA part of the recognition signal for ribosomal initiation? Nucleic Acids Res. 1979 Oct 25;7(4):1035–1041. doi: 10.1093/nar/7.4.1035. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Atkins J. F., Steitz J. A., Anderson C. W., Model P. Binding of mammalian ribosomes to MS2 phage RNA reveals an overlapping gene encoding a lysis function. Cell. 1979 Oct;18(2):247–256. doi: 10.1016/0092-8674(79)90044-8. [DOI] [PubMed] [Google Scholar]
  13. Backendorf C., Ravensbergen C. J., Van der Plas J., van Boom J. H., Veeneman G., Van Duin J. Basepairing potential of the 3' terminus of 16S RNA: dependence on the functional state of the 30S subunit and the presence of protein S21. Nucleic Acids Res. 1981 Mar 25;9(6):1425–1444. doi: 10.1093/nar/9.6.1425. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Bahramian M. B. How bacterial ribosomes select translation initiation sites. J Theor Biol. 1980 May 7;84(1):103–118. doi: 10.1016/s0022-5193(80)81039-3. [DOI] [PubMed] [Google Scholar]
  15. Baker C. C., Herisse J., Courtois G., Galibert F., Ziff E. Messenger RNA for the Ad2 DNA binding protein: DNA sequences encoding the first leader and heterogenity at the mRNA 5' end. Cell. 1979 Oct;18(2):569–580. doi: 10.1016/0092-8674(79)90073-4. [DOI] [PubMed] [Google Scholar]
  16. Baker C. C., Ziff E. B. Promoters and heterogeneous 5' termini of the messenger RNAs of adenovirus serotype 2. J Mol Biol. 1981 Jun 25;149(2):189–221. doi: 10.1016/0022-2836(81)90298-9. [DOI] [PubMed] [Google Scholar]
  17. Banerjee A. K. 5'-terminal cap structure in eucaryotic messenger ribonucleic acids. Microbiol Rev. 1980 Jun;44(2):175–205. doi: 10.1128/mr.44.2.175-205.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Barrell B. G., Bankier A. T., Drouin J. A different genetic code in human mitochondria. Nature. 1979 Nov 8;282(5735):189–194. doi: 10.1038/282189a0. [DOI] [PubMed] [Google Scholar]
  19. Barry G., Squires C., Squires C. L. Attenuation and processing of RNA from the rplJL--rpoBC transcription unit of Escherichia coli. Proc Natl Acad Sci U S A. 1980 Jun;77(6):3331–3335. doi: 10.1073/pnas.77.6.3331. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Baumstark B. R., Spremulli L. L., RajBhandary U. L., Brown G. M. Initiation of protein synthesis without formylation in a mutant of Escherichia coli that grows in the absence of tetrahydrofolate. J Bacteriol. 1977 Jan;129(1):457–471. doi: 10.1128/jb.129.1.457-471.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Beemon K., Hunter T. In vitro translation yields a possible Rous sarcoma virus src gene product. Proc Natl Acad Sci U S A. 1977 Aug;74(8):3302–3306. doi: 10.1073/pnas.74.8.3302. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Belin D., Hedgpeth J., Selzer G. B., Epstein R. H. Temperature-sensitive mutation in the initiation codon of the rIIB gene of bacteriophage T4. Proc Natl Acad Sci U S A. 1979 Feb;76(2):700–704. doi: 10.1073/pnas.76.2.700. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Bellemare G., Vigne R., Jordan B. R. Interaction between Escherichia coli ribosomal proteins and 5S RNA molecules: recognition of prokaryotic 5S RNAs and rejection of eukaryotic 5S RNAs. Biochimie. 1973;55(1):29–35. doi: 10.1016/s0300-9084(73)80233-0. [DOI] [PubMed] [Google Scholar]
  24. Benne R., Amesz H., Hershey J. W., Voorma H. O. The activity of eukaryotic initiation factor eIF-2 in ternary complex formation with GTP and Met-tRNA. J Biol Chem. 1979 May 10;254(9):3201–3205. [PubMed] [Google Scholar]
  25. Benne R., Arentzen R., Voorma H. O. The mechanism of action of inititation factor F1 from Escherichia coli. Biochim Biophys Acta. 1972 May 10;269(2):304–310. doi: 10.1016/0005-2787(72)90440-6. [DOI] [PubMed] [Google Scholar]
  26. Benne R., Hershey J. W. The mechanism of action of protein synthesis initiation factors from rabbit reticulocytes. J Biol Chem. 1978 May 10;253(9):3078–3087. [PubMed] [Google Scholar]
  27. Bennetzen J. L., Hall B. D. Codon selection in yeast. J Biol Chem. 1982 Mar 25;257(6):3026–3031. [PubMed] [Google Scholar]
  28. Bennetzen J. L., Hall B. D. The primary structure of the Saccharomyces cerevisiae gene for alcohol dehydrogenase. J Biol Chem. 1982 Mar 25;257(6):3018–3025. [PubMed] [Google Scholar]
  29. Berissi H., Groner Y., Revel M. Effect of a purified initiation factor F3 (B) on the selection of ribosomal binding sites on phage MS2 RNA. Nat New Biol. 1971 Nov 10;234(45):44–47. doi: 10.1038/newbio234044a0. [DOI] [PubMed] [Google Scholar]
  30. Bernardi A., Spahr P. F. Nucleotide sequence at the binding site for coat protein on RNA of bacteriophage R17. Proc Natl Acad Sci U S A. 1972 Oct;69(10):3033–3037. doi: 10.1073/pnas.69.10.3033. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Bibb M. J., Van Etten R. A., Wright C. T., Walberg M. W., Clayton D. A. Sequence and gene organization of mouse mitochondrial DNA. Cell. 1981 Oct;26(2 Pt 2):167–180. doi: 10.1016/0092-8674(81)90300-7. [DOI] [PubMed] [Google Scholar]
  32. Bishop D. H., Gould K. G., Akashi H., Clerx-van Haaster C. M. The complete sequence and coding content of snowshoe hare bunyavirus small (S) viral RNA species. Nucleic Acids Res. 1982 Jun 25;10(12):3703–3713. doi: 10.1093/nar/10.12.3703. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. Blackburn D. E., Hobbs A. A., Rosen J. M. Rat beta casein cDNA: sequence analysis and evolutionary comparisons. Nucleic Acids Res. 1982 Apr 10;10(7):2295–2307. doi: 10.1093/nar/10.7.2295. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. Bonen L., Cunningham R. S., Gray M. W., Doolittle W. F. Wheat embryo mitochondrial 18S ribosomal RNA: evidence for its prokaryotic nature. Nucleic Acids Res. 1977 Mar;4(3):663–671. doi: 10.1093/nar/4.3.663. [DOI] [PMC free article] [PubMed] [Google Scholar]
  35. Bonitz S. G., Berlani R., Coruzzi G., Li M., Macino G., Nobrega F. G., Nobrega M. P., Thalenfeld B. E., Tzagoloff A. Codon recognition rules in yeast mitochondria. Proc Natl Acad Sci U S A. 1980 Jun;77(6):3167–3170. doi: 10.1073/pnas.77.6.3167. [DOI] [PMC free article] [PubMed] [Google Scholar]
  36. Borisova G. P., Volkova T. M., Berzin V., Rosenthal G., Gren E. J. The regulatory region of MS2 phage RNA replicase cistron. IV. Functional activity of specific MS2 RNA fragments in formation of the 70 S initiation complex of protein biosynthesis. Nucleic Acids Res. 1979;6(5):1761–1774. doi: 10.1093/nar/6.5.1761. [DOI] [PMC free article] [PubMed] [Google Scholar]
  37. Borst P., Grivell L. A. The mitochondrial genome of yeast. Cell. 1978 Nov;15(3):705–723. doi: 10.1016/0092-8674(78)90257-x. [DOI] [PubMed] [Google Scholar]
  38. Bos J. L., Osinga K. A., Van der Horst G., Hecht N. B., Tabak H. F., Van Ommen G. J., Borst P. Splice point sequence and transcripts of the intervening sequence in the mitochondrial 21S ribosomal RNA gene of yeast. Cell. 1980 May;20(1):207–214. doi: 10.1016/0092-8674(80)90248-2. [DOI] [PubMed] [Google Scholar]
  39. Bos J. L., Polder L. J., Bernards R., Schrier P. I., van den Elsen P. J., van der Eb A. J., van Ormondt H. The 2.2 kb E1b mRNA of human Ad12 and Ad5 codes for two tumor antigens starting at different AUG triplets. Cell. 1981 Nov;27(1 Pt 2):121–131. doi: 10.1016/0092-8674(81)90366-4. [DOI] [PubMed] [Google Scholar]
  40. Boulik M., Hellmann W. Comparison of Artemia salina and Escherichia coli ribosome structure by electron microscopy. Proc Natl Acad Sci U S A. 1978 Jun;75(6):2829–2833. doi: 10.1073/pnas.75.6.2829. [DOI] [PMC free article] [PubMed] [Google Scholar]
  41. Brawner M. E., Jaskunas S. R. Identification of polypeptides encoded by the replication of resistance factor R100. J Mol Biol. 1982 Jul 25;159(1):35–55. doi: 10.1016/0022-2836(82)90030-4. [DOI] [PubMed] [Google Scholar]
  42. Breathnach R., Chambon P. Organization and expression of eucaryotic split genes coding for proteins. Annu Rev Biochem. 1981;50:349–383. doi: 10.1146/annurev.bi.50.070181.002025. [DOI] [PubMed] [Google Scholar]
  43. Bretscher M. S. Direct translation of bacteriophage fd DNA in the absence of neomycin B. J Mol Biol. 1969 Jun 28;42(3):595–598. doi: 10.1016/0022-2836(69)90247-2. [DOI] [PubMed] [Google Scholar]
  44. Brimacombe R., Stöffler G., Wittmann H. G. Ribosome structure. Annu Rev Biochem. 1978;47:217–249. doi: 10.1146/annurev.bi.47.070178.001245. [DOI] [PubMed] [Google Scholar]
  45. Brosius J., Dull T. J., Noller H. F. Complete nucleotide sequence of a 23S ribosomal RNA gene from Escherichia coli. Proc Natl Acad Sci U S A. 1980 Jan;77(1):201–204. doi: 10.1073/pnas.77.1.201. [DOI] [PMC free article] [PubMed] [Google Scholar]
  46. Brown J. C., Smith A. E. Initiator codons in eukaryotes. Nature. 1970 May 16;226(5246):610–612. doi: 10.1038/226610a0. [DOI] [PubMed] [Google Scholar]
  47. Brown J. L., Roberts W. K. Evidence that approximately eighty per cent of the soluble proteins from Ehrlich ascites cells are Nalpha-acetylated. J Biol Chem. 1976 Feb 25;251(4):1009–1014. [PubMed] [Google Scholar]
  48. Browning K. S., RajBhandary U. L. Cytochrome oxidase subunit III gene in Neurospora crassa mitochondria. Location and sequence. J Biol Chem. 1982 May 10;257(9):5253–5256. [PubMed] [Google Scholar]
  49. Buetow D. E., Wood W. M. The mitochondrial translation system. Subcell Biochem. 1978;5:1–85. doi: 10.1007/978-1-4615-7942-7_1. [DOI] [PubMed] [Google Scholar]
  50. Calagan J. L., Pirtle R. M., Pirtle I. L., Kashdan M. A., Vreman H. J., Dudock B. S. Homology between chloroplast and prokaryotic initiator tRNA. Nucleotide sequence of spinach chloroplast methionine initiator tRNA. J Biol Chem. 1980 Oct 25;255(20):9981–9984. [PubMed] [Google Scholar]
  51. Campbell G. R., Littau V. C., Melera P. W., Allfrey V. G., Johnson E. M. Unique sequence arrangement of ribosomal genes in the palindromic rDNA molecule of Physarum polycephalum. Nucleic Acids Res. 1979 Apr;6(4):1433–1447. doi: 10.1093/nar/6.4.1433. [DOI] [PMC free article] [PubMed] [Google Scholar]
  52. Canaday J., Dirheimer G., Martin R. P. Yeast mitochondrial methionine initiator tRNA: characterization and nucleotide sequence. Nucleic Acids Res. 1980 Apr 11;8(7):1445–1457. doi: 10.1093/nar/8.7.1445. [DOI] [PMC free article] [PubMed] [Google Scholar]
  53. Cannistraro V. J., Kennell D. Escherichia coli lac operator mRNA affects translation initiation of beta-galactosidase mRNA. Nature. 1979 Feb 1;277(5695):407–409. doi: 10.1038/277407a0. [DOI] [PubMed] [Google Scholar]
  54. Capel M. S., Bourque D. P. Characterization of Nicotiana tabacum chloroplast and cytoplasmic ribosomal proteins. J Biol Chem. 1982 Jul 10;257(13):7746–7755. [PubMed] [Google Scholar]
  55. Carlson M., Botstein D. Two differentially regulated mRNAs with different 5' ends encode secreted with intracellular forms of yeast invertase. Cell. 1982 Jan;28(1):145–154. doi: 10.1016/0092-8674(82)90384-1. [DOI] [PubMed] [Google Scholar]
  56. Caskey C. T., Beaudet A., Nirenberg M. RNA codons and protein synthesis. 15. Dissimilar responses of mammalian and bacterial transfer RNA fractions to messenger RNA codons. J Mol Biol. 1968 Oct 14;37(1):99–118. doi: 10.1016/0022-2836(68)90076-4. [DOI] [PubMed] [Google Scholar]
  57. Castel A., Kraal B., Konieczny A., Bosch L. Translation by Escherichia coli ribosomes of alfalfa mosaic virus RNA 4 can be initiated at two sites on the monocistronic message. Eur J Biochem. 1979 Nov 1;101(1):123–133. doi: 10.1111/j.1432-1033.1979.tb04224.x. [DOI] [PubMed] [Google Scholar]
  58. Catterall J. F., O'Malley B. W., Robertson M. A., Staden R., Tanaka Y., Brownlee G. G. Nucleotide sequence homology at 12 intron--exon junctions in the chick ovalbumin gene. Nature. 1978 Oct 12;275(5680):510–513. doi: 10.1038/275510a0. [DOI] [PubMed] [Google Scholar]
  59. Cepko C. L., Hansen U., Handa H., Sharp P. A. Sequential transcription-translation of simian virus 40 by using mammalian cell extracts. Mol Cell Biol. 1981 Oct;1(10):919–931. doi: 10.1128/mcb.1.10.919. [DOI] [PMC free article] [PubMed] [Google Scholar]
  60. Chaires J. B., Pande C., Wishnia A. The effect of initiation factor IF-3 on Escherichia coli ribosomal subunit association kinetics. J Biol Chem. 1981 Jul 10;256(13):6600–6607. [PubMed] [Google Scholar]
  61. Chapon C. Expression of malT, the regulator gene of the maltose region in Escherichia coli, is limited both at transcription and translation. EMBO J. 1982;1(3):369–374. doi: 10.1002/j.1460-2075.1982.tb01176.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  62. Chaudhuri A., Stringer E. A., Valenzuela D., Maitra U. Characterization of eukaryotic initiation factor 2 containing two polypeptide chains of Mr = 48,000 and 38,000. J Biol Chem. 1981 Apr 25;256(8):3988–3994. [PubMed] [Google Scholar]
  63. Chin W. W., Kronenberg H. M., Dee P. C., Maloof F., Habener J. F. Nucleotide sequence of the mRNA encoding the pre-alpha-subunit of mouse thyrotropin. Proc Natl Acad Sci U S A. 1981 Sep;78(9):5329–5333. doi: 10.1073/pnas.78.9.5329. [DOI] [PMC free article] [PubMed] [Google Scholar]
  64. Choe J., Kolodrubetz D., Grunstein M. The two yeast histone H2A genes encode similar protein subtypes. Proc Natl Acad Sci U S A. 1982 Mar;79(5):1484–1487. doi: 10.1073/pnas.79.5.1484. [DOI] [PMC free article] [PubMed] [Google Scholar]
  65. Chow L. T., Broker T. R., Lewis J. B. Complex splicing patterns of RNAs from the early regions of adenovirus-2. J Mol Biol. 1979 Oct 25;134(2):265–303. doi: 10.1016/0022-2836(79)90036-6. [DOI] [PubMed] [Google Scholar]
  66. Christie G. E., Platt T. Gene structure in the tryptophan operon of Escherichia coli. Nucleotide sequence of trpC and the flanking intercistronic regions. J Mol Biol. 1980 Oct 5;142(4):519–530. doi: 10.1016/0022-2836(80)90261-2. [DOI] [PubMed] [Google Scholar]
  67. Clark B. F., Marcker K. A. The role of N-formyl-methionyl-sRNA in protein biosynthesis. J Mol Biol. 1966 Jun;17(2):394–406. doi: 10.1016/s0022-2836(66)80150-x. [DOI] [PubMed] [Google Scholar]
  68. Clemens M. J., Pain V. M., Wong S. T., Henshaw E. C. Phosphorylation inhibits guanine nucleotide exchange on eukaryotic initiation factor 2. Nature. 1982 Mar 4;296(5852):93–95. doi: 10.1038/296093a0. [DOI] [PubMed] [Google Scholar]
  69. Clerx-van Haaster C. M., Akashi H., Auperin D. D., Bishop D. H. Nucleotide sequence analyses and predicted coding of bunyavirus genome RNA species. J Virol. 1982 Jan;41(1):119–128. doi: 10.1128/jvi.41.1.119-128.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  70. Cole S. T. Nucleotide sequence coding for the flavoprotein subunit of the fumarate reductase of Escherichia coli. Eur J Biochem. 1982 Mar 1;122(3):479–484. doi: 10.1111/j.1432-1033.1982.tb06462.x. [DOI] [PubMed] [Google Scholar]
  71. Collins P. L., Fuller F. J., Marcus P. I., Hightower L. E., Ball L. A. Synthesis and processing of Sindbis virus nonstructural proteins in vitro. Virology. 1982 Apr 30;118(2):363–379. doi: 10.1016/0042-6822(82)90356-7. [DOI] [PubMed] [Google Scholar]
  72. Cordell B., Diamond D., Smith S., Pünter J., Schöne H. H., Goodman H. M. Disproportionate expression of the two nonallelic rat insulin genes in a pancreatic tumor is due to translational control. Cell. 1982 Dec;31(3 Pt 2):531–542. doi: 10.1016/0092-8674(82)90309-9. [DOI] [PubMed] [Google Scholar]
  73. Coruzzi G., Bonitz S. G., Thalenfeld B. E., Tzagoloff A. Assembly of the mitochondrial membrane system. Analysis of the nucleotide sequence and transcripts in the oxi1 region of yeast mitochondrial DNA. J Biol Chem. 1981 Dec 25;256(24):12780–12787. [PubMed] [Google Scholar]
  74. Cowie A., Tyndall C., Kamen R. Sequences at the capped 5'-ends of polyoma virus late region mRNAs: an example of extreme terminal heterogeneity. Nucleic Acids Res. 1981 Dec 11;9(23):6305–6322. doi: 10.1093/nar/9.23.6305. [DOI] [PMC free article] [PubMed] [Google Scholar]
  75. Darlix J. L., Spahr P. F., Bromley P. A., Jaton J. C. In vitro, the major ribosome binding site on Rous sarcoma virus RNA does not contain the nucleotide sequence coding for the N-terminal amino acids of the gag gene product. J Virol. 1979 Feb;29(2):597–611. doi: 10.1128/jvi.29.2.597-611.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  76. Davies J. W., Kaesberg P. Translation of virus mRNA: synthesis of bacteriophage Q beta proteins in a cell-free extract from wheat embryo. J Virol. 1973 Dec;12(6):1434–1441. doi: 10.1128/jvi.12.6.1434-1441.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  77. De Ronde A., Van Loon A. P., Grivell L. A., Kohli J. In vitro suppression of UGA codons in a mitochondrial mRNA. Nature. 1980 Sep 25;287(5780):361–363. doi: 10.1038/287361a0. [DOI] [PubMed] [Google Scholar]
  78. Derynck R., Leung D. W., Gray P. W., Goeddel D. V. Human interferon gamma is encoded by a single class of mRNA. Nucleic Acids Res. 1982 Jun 25;10(12):3605–3615. doi: 10.1093/nar/10.12.3605. [DOI] [PMC free article] [PubMed] [Google Scholar]
  79. Devine J. M., Williams J. G. Characterization of sequence elements at the 5' end of a discoidin I gene isolated from Dictyostelium discoideum. Nucleic Acids Res. 1982 Feb 25;10(4):1231–1241. doi: 10.1093/nar/10.4.1231. [DOI] [PMC free article] [PubMed] [Google Scholar]
  80. Dimock K., Stoltzfus C. M. Processing and function of undermethylated chicken embryo fibroblast mRNA. J Biol Chem. 1979 Jul 10;254(13):5591–5594. [PubMed] [Google Scholar]
  81. Dubin D. T., Timko K. D., Baer R. J. The 3' terminus of the large ribosomal subunit ("17S") RNA from hamster mitochondria is ragged and oligoadenylated. Cell. 1981 Jan;23(1):271–278. doi: 10.1016/0092-8674(81)90291-9. [DOI] [PubMed] [Google Scholar]
  82. Dubnoff J. S., Lockwood A. H., Maitra U. Studies on the role of guanosine triphosphate in polypeptide chain initiation in Escherichia coli. J Biol Chem. 1972 May 10;247(9):2884–2894. [PubMed] [Google Scholar]
  83. Dugaiczyk A., Law S. W., Dennison O. E. Nucleotide sequence and the encoded amino acids of human serum albumin mRNA. Proc Natl Acad Sci U S A. 1982 Jan;79(1):71–75. doi: 10.1073/pnas.79.1.71. [DOI] [PMC free article] [PubMed] [Google Scholar]
  84. Dunn J. J., Buzash-Pollert E., Studier F. W. Mutations of bacteriophage T7 that affect initiation of synthesis of the gene 0.3 protein. Proc Natl Acad Sci U S A. 1978 Jun;75(6):2741–2745. doi: 10.1073/pnas.75.6.2741. [DOI] [PMC free article] [PubMed] [Google Scholar]
  85. Dunn J. J., Studier F. W. Effect of RNAase III, cleavage on translation of bacteriophage T7 messenger RNAs. J Mol Biol. 1975 Dec 15;99(3):487–499. doi: 10.1016/s0022-2836(75)80140-9. [DOI] [PubMed] [Google Scholar]
  86. Dunn J. J., Studier F. W. Nucleotide sequence from the genetic left end of bacteriophage T7 DNA to the beginning of gene 4. J Mol Biol. 1981 Jun 5;148(4):303–330. doi: 10.1016/0022-2836(81)90178-9. [DOI] [PubMed] [Google Scholar]
  87. Dyer T. A., Bowman C. M. Nucleotide sequences of chloroplast 5S ribosomal ribonucleic acid in flowering plants. Biochem J. 1979 Dec 1;183(3):595–604. doi: 10.1042/bj1830595. [DOI] [PMC free article] [PubMed] [Google Scholar]
  88. Eckhardt H., Lührmann R. Recognition by initiator transfer ribonucleic acid of a uridine 5' adjacent to the AUG codon: different conformational states of formylatable methionine-accepting transfer ribonucleic acid at the ribosomal peptidyl site. Biochemistry. 1981 Apr 14;20(8):2075–2080. doi: 10.1021/bi00511a002. [DOI] [PubMed] [Google Scholar]
  89. Emtage J. S., Tacon W. C., Catlin G. H., Jenkins B., Porter A. G., Carey N. H. Influenza antigenic determinants are expressed from haemagglutinin genes cloned in Escherichia coli. Nature. 1980 Jan 10;283(5743):171–174. doi: 10.1038/283171a0. [DOI] [PubMed] [Google Scholar]
  90. Eperon I. C., Anderson S., Nierlich D. P. Distinctive sequence of human mitochondrial ribosomal RNA genes. Nature. 1980 Jul 31;286(5772):460–467. doi: 10.1038/286460a0. [DOI] [PubMed] [Google Scholar]
  91. Faye G., Leung D. W., Tatchell K., Hall B. D., Smith M. Deletion mapping of sequences essential for in vivo transcription of the iso-1-cytochrome c gene. Proc Natl Acad Sci U S A. 1981 Apr;78(4):2258–2262. doi: 10.1073/pnas.78.4.2258. [DOI] [PMC free article] [PubMed] [Google Scholar]
  92. Faye G., Sor F. Analysis of mitochondrial ribosomal proteins of Saccharomyces cerevisiae by two dimensional polyacrylamide gel electrophoresis. Mol Gen Genet. 1977 Sep 21;155(1):27–34. doi: 10.1007/BF00268557. [DOI] [PubMed] [Google Scholar]
  93. Fiddes J. C., Goodman H. M. The gene encoding the common alpha subunit of the four human glycoprotein hormones. J Mol Appl Genet. 1981;1(1):3–18. [PubMed] [Google Scholar]
  94. Fischer N., Stöffler G., Wool I. G. Immunological comparison of the proteins of chicken and rat liver ribosomes. J Biol Chem. 1978 Oct 25;253(20):7355–7360. [PubMed] [Google Scholar]
  95. Fried H. M., Pearson N. J., Kim C. H., Warner J. R. The genes for fifteen ribosomal proteins of Saccharomyces cerevisiae. J Biol Chem. 1981 Oct 10;256(19):10176–10183. [PubMed] [Google Scholar]
  96. Gallwitz D., Perrin F., Seidel R. The actin gene in yeast Saccharomyces cerevisiae: 5' and 3' end mapping, flanking and putative regulatory sequences. Nucleic Acids Res. 1981 Dec 11;9(23):6339–6350. doi: 10.1093/nar/9.23.6339. [DOI] [PMC free article] [PubMed] [Google Scholar]
  97. Ganoza M. C., Sullivan P., Cunningham C., Hader P., Kofoid E. C., Neilson T. Effect of bases contiguous to AUG on translation initiation. J Biol Chem. 1982 Jul 25;257(14):8228–8232. [PubMed] [Google Scholar]
  98. Gatenby A. A., Castleton J. A., Saul M. W. Expression in E. coli of maize and wheat chloroplast genes for large subunit of ribulose bisphosphate carboxylase. Nature. 1981 May 14;291(5811):117–121. doi: 10.1038/291117a0. [DOI] [PubMed] [Google Scholar]
  99. Gauss D. H., Grüter F., Sprinzl M. Compilation of tRNA sequences. Nucleic Acids Res. 1979 Jan;6(1):r1–r19. [PMC free article] [PubMed] [Google Scholar]
  100. Gay N. J., Walker J. E. The atp operon: nucleotide sequence of the promoter and the genes for the membrane proteins, and the delta subunit of Escherichia coli ATP-synthase. Nucleic Acids Res. 1981 Aug 25;9(16):3919–3926. doi: 10.1093/nar/9.16.3919. [DOI] [PMC free article] [PubMed] [Google Scholar]
  101. Gegenheimer P., Apirion D. Processing of procaryotic ribonucleic acid. Microbiol Rev. 1981 Dec;45(4):502–541. doi: 10.1128/mr.45.4.502-541.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  102. Gette W. R., Heywood S. M. Translation of myosin heavy chain messenger ribonucleic acid in an eukaryotic initiation factor 3- and messenger-dependent muscle cell-free system. J Biol Chem. 1979 Oct 10;254(19):9879–9885. [PubMed] [Google Scholar]
  103. Geyer P. K., Meyuhas O., Perry R. P., Johnson L. F. Regulation of ribosomal protein mRNA content and translation in growth-stimulated mouse fibroblasts. Mol Cell Biol. 1982 Jun;2(6):685–693. doi: 10.1128/mcb.2.6.685. [DOI] [PMC free article] [PubMed] [Google Scholar]
  104. Gheysen D., Iserentant D., Derom C., Fiers W. Systematic alteration of the nucleotide sequence preceding the translation initiation codon and the effects on bacterial expression of the cloned SV40 small-t antigen gene. Gene. 1982 Jan;17(1):55–63. doi: 10.1016/0378-1119(82)90100-7. [DOI] [PubMed] [Google Scholar]
  105. Ghosh H. P., Ghosh K., Simsek M., RajBhandary U. L. Nucleotide sequence of wheat germ cytoplasmic initiator methionine transfer ribonucleic acid. Nucleic Acids Res. 1982 May 25;10(10):3241–3247. doi: 10.1093/nar/10.10.3241. [DOI] [PMC free article] [PubMed] [Google Scholar]
  106. Ghosh K., Ghosh H. P., Simsek M., Raj Bhandary U. L. Initiator methionine transfer ribonucleic acid from wheat embryo. Purification, properties, and partial nucleotide sequences. J Biol Chem. 1974 Aug 10;249(15):4720–4729. [PubMed] [Google Scholar]
  107. Ghosh P. K., Lebowitz P. Simian virus 40 early mRNA's contain multiple 5' termini upstream and downstream from a Hogness-Goldberg sequence; a shift in 5' termini during the lytic cycle is mediated by large T antigen. J Virol. 1981 Oct;40(1):224–240. doi: 10.1128/jvi.40.1.224-240.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  108. Gillam S., Astell C. R., Smith M. Site-specific mutagenesis using oligodeoxyribonucleotides: isolation of a phenotypically silent phi X174 mutant, with a specific nucleotide deletion, at very high efficiency. Gene. 1980 Dec;12(1-2):129–137. doi: 10.1016/0378-1119(80)90023-2. [DOI] [PubMed] [Google Scholar]
  109. Gitelman D. R., Apirion D. The synthesis of some proteins is affected in RNA processing mutants of Escherichia coli. Biochem Biophys Res Commun. 1980 Oct 16;96(3):1063–1070. doi: 10.1016/0006-291x(80)90060-1. [DOI] [PubMed] [Google Scholar]
  110. Givol D., Zakut R., Effron K., Rechavi G., Ram D., Cohen J. B. Diversity of germ-line immunoglobulin VH genes. Nature. 1981 Jul 30;292(5822):426–430. doi: 10.1038/292426a0. [DOI] [PubMed] [Google Scholar]
  111. Glanville N., Ranki M., Morser J., Käriäinen L., Smith A. E. Initiation of translation directed by 42S and 26S RNAs from Semliki Forest virus in vitro. Proc Natl Acad Sci U S A. 1976 Sep;73(9):3059–3063. doi: 10.1073/pnas.73.9.3059. [DOI] [PMC free article] [PubMed] [Google Scholar]
  112. Glover J. F., Wilson T. M. Efficient translation of the coat protein cistron of tobacco mosaic virus in a cell-free system from Escherichia coli. Eur J Biochem. 1982 Mar 1;122(3):485–492. doi: 10.1111/j.1432-1033.1982.tb06463.x. [DOI] [PubMed] [Google Scholar]
  113. Godefroy-Colburn T., Thach R. E. The role of mRNA competition in regulating translation. IV. Kinetic model. J Biol Chem. 1981 Nov 25;256(22):11762–11773. [PubMed] [Google Scholar]
  114. Godine J. E., Chin W. W., Habener J. F. alpha Subunit of rat pituitary glycoprotein hormones. Primary structure of the precursor determined from the nucleotide sequence of cloned cDNAs. J Biol Chem. 1982 Jul 25;257(14):8368–8371. [PubMed] [Google Scholar]
  115. Godson G. N., Barrell B. G., Staden R., Fiddes J. C. Nucleotide sequence of bacteriophage G4 DNA. Nature. 1978 Nov 16;276(5685):236–247. doi: 10.1038/276236a0. [DOI] [PubMed] [Google Scholar]
  116. Gold L., Pribnow D., Schneider T., Shinedling S., Singer B. S., Stormo G. Translational initiation in prokaryotes. Annu Rev Microbiol. 1981;35:365–403. doi: 10.1146/annurev.mi.35.100181.002053. [DOI] [PubMed] [Google Scholar]
  117. Goldberg M. L., Steitz J. A. Cistron specificity of 30S ribosomes heterologously reconstituted with components from Escherichia coli and Bacillus stearothermophilus. Biochemistry. 1974 May 7;13(10):2123–2129. doi: 10.1021/bi00707a020. [DOI] [PubMed] [Google Scholar]
  118. Golini F., Semler B. L., Dorner A. J., Wimmer E. Protein-linked RNA of poliovirus is competent to form an initiation complex of translation in vitro. Nature. 1980 Oct 16;287(5783):600–603. doi: 10.1038/287600a0. [DOI] [PubMed] [Google Scholar]
  119. Golini F., Thach S. S., Birge C. H., Safer B., Merrick W. C., Thach R. E. Competition between cellular and viral mRNAs in vitro is regulated by a messenger discriminatory initiation factor. Proc Natl Acad Sci U S A. 1976 Sep;73(9):3040–3044. doi: 10.1073/pnas.73.9.3040. [DOI] [PMC free article] [PubMed] [Google Scholar]
  120. Gopalakrishna Y., Langley D., Sarkar N. Detection of high levels of polyadenylate-containing RNA in bacteria by the use of a single-step RNA isolation procedure. Nucleic Acids Res. 1981 Jul 24;9(14):3545–3554. doi: 10.1093/nar/9.14.3545. [DOI] [PMC free article] [PubMed] [Google Scholar]
  121. Gopalakrishna Y., Sarkar N. Characterization of polyadenylate-containing ribonucleic acid from Bacillus subtilis. Biochemistry. 1982 May 25;21(11):2724–2729. doi: 10.1021/bi00540a023. [DOI] [PubMed] [Google Scholar]
  122. Gorenstein C., Warner J. R. Coordinate regulation of the synthesis of eukaryotic ribosomal proteins. Proc Natl Acad Sci U S A. 1976 May;73(5):1547–1551. doi: 10.1073/pnas.73.5.1547. [DOI] [PMC free article] [PubMed] [Google Scholar]
  123. Gottesman M., Oppenheim A., Court D. Retroregulation: control of gene expression from sites distal to the gene. Cell. 1982 Jul;29(3):727–728. doi: 10.1016/0092-8674(82)90434-2. [DOI] [PubMed] [Google Scholar]
  124. Goumans H., Thomas A., Verhoeven A., Voorma H. O., Benne R. The role of eIF-4C in protein synthesis initiation complex formation. Biochim Biophys Acta. 1980 Jun 27;608(1):39–46. doi: 10.1016/0005-2787(80)90131-8. [DOI] [PubMed] [Google Scholar]
  125. Gourse R. L., Thurlow D. L., Gerbi S. A., Zimmermann R. A. Specific binding of a prokaryotic ribosomal protein to a eukaryotic ribosomal RNA: implications for evolution and autoregulation. Proc Natl Acad Sci U S A. 1981 May;78(5):2722–2726. doi: 10.1073/pnas.78.5.2722. [DOI] [PMC free article] [PubMed] [Google Scholar]
  126. Graves M. C., Breitenberger C. A., Spremulli L. L. Euglena gracilis chloroplast ribosomes: improved isolation procedure and comparison of elongation factor specificity with prokaryotic and eukaryotic ribosomes. Arch Biochem Biophys. 1980 Oct 15;204(2):444–454. doi: 10.1016/0003-9861(80)90055-7. [DOI] [PubMed] [Google Scholar]
  127. Gray M. W., Doolittle W. F. Has the endosymbiont hypothesis been proven? Microbiol Rev. 1982 Mar;46(1):1–42. doi: 10.1128/mr.46.1.1-42.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  128. Gray M. W. Mitochondrial genome diversity and the evolution of mitochondrial DNA. Can J Biochem. 1982 Mar;60(3):157–171. doi: 10.1139/o82-022. [DOI] [PubMed] [Google Scholar]
  129. Grez M., Land H., Giesecke K., Schütz G., Jung A., Sippel A. E. Multiple mRNAs are generated from the chicken lysozyme gene. Cell. 1981 Sep;25(3):743–752. doi: 10.1016/0092-8674(81)90182-3. [DOI] [PubMed] [Google Scholar]
  130. Grifo J. A., Tahara S. M., Leis J. P., Morgan M. A., Shatkin A. J., Merrick W. C. Characterization of eukaryotic initiation factor 4A, a protein involved in ATP-dependent binding of globin mRNA. J Biol Chem. 1982 May 10;257(9):5246–5252. [PubMed] [Google Scholar]
  131. Grivell L. A., Walg H. L. Subunit homology between Escherichia coli, mitochondrial and chloroplast ribosomes. Biochem Biophys Res Commun. 1972 Dec 18;49(6):1452–1458. doi: 10.1016/0006-291x(72)90502-5. [DOI] [PubMed] [Google Scholar]
  132. Grohmann K., Amairic F., Crews S., Attardi G. Failure to detect "cap" structures in mitochondrial DNA-coded poly(A)-containing RNA from HeLa cells. Nucleic Acids Res. 1978 Mar;5(3):637–651. doi: 10.1093/nar/5.3.637. [DOI] [PMC free article] [PubMed] [Google Scholar]
  133. Gualerzi C., Risuleo G., Pon C. L. Initial rate kinetic analysis of the mechanism of initiation complex formation and the role of initiation factor IF-3. Biochemistry. 1977 Apr 19;16(8):1684–1689. doi: 10.1021/bi00627a025. [DOI] [PubMed] [Google Scholar]
  134. Guarente L., Lauer G., Roberts T. M., Ptashne M. Improved methods for maximizing expression of a cloned gene: a bacterium that synthesizes rabbit beta-globin. Cell. 1980 Jun;20(2):543–553. doi: 10.1016/0092-8674(80)90640-6. [DOI] [PubMed] [Google Scholar]
  135. Hackett P. B., Egberts E., Traub P. Characterization of Ehrlich ascites tumor cell messenger RNA specifying ribosomal proteins by translation in vitro. J Mol Biol. 1978 Feb 25;119(2):253–267. doi: 10.1016/0022-2836(78)90437-0. [DOI] [PubMed] [Google Scholar]
  136. Hagen F. S., Young E. T. Effect of RNase III on efficiency of translation of bacteriophage T7 lysozyme mRNA. J Virol. 1978 Jun;26(3):793–804. doi: 10.1128/jvi.26.3.793-804.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  137. Hagenbüchle O., Santer M., Steitz J. A., Mans R. J. Conservation of the primary structure at the 3' end of 18S rRNA from eucaryotic cells. Cell. 1978 Mar;13(3):551–563. doi: 10.1016/0092-8674(78)90328-8. [DOI] [PubMed] [Google Scholar]
  138. Halbreich A., Rabinowitz M. Isolation of Saccharomyces cerevisiae mitochondrial formyltetrahydrofolic acid:methionyl-tRNA transformylase and the hybridization of mitochondrial fMet-tRNA with mitochondrial DNA. Proc Natl Acad Sci U S A. 1971 Feb;68(2):294–298. doi: 10.1073/pnas.68.2.294. [DOI] [PMC free article] [PubMed] [Google Scholar]
  139. Hall L. M., Maden B. E. Nucleotide sequence through the 18S-28S intergene region of a vertebrate ribosomal transcription unit. Nucleic Acids Res. 1980 Dec 20;8(24):5993–6005. doi: 10.1093/nar/8.24.5993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  140. Hall L., Craig R. K., Edbrooke M. R., Campbell P. N. Comparison of the nucleotide sequence of cloned human and guinea-pig pre-alpha-lactalbumin cDNA with that of chick pre-lysozyme cDNA suggests evolution from a common ancestral gene. Nucleic Acids Res. 1982 Jun 11;10(11):3503–3515. doi: 10.1093/nar/10.11.3503. [DOI] [PMC free article] [PubMed] [Google Scholar]
  141. Hall M. N., Gabay J., Débarbouillé M., Schwartz M. A role for mRNA secondary structure in the control of translation initiation. Nature. 1982 Feb 18;295(5850):616–618. doi: 10.1038/295616a0. [DOI] [PubMed] [Google Scholar]
  142. Hartley M. R. The synthesis and origin of chloroplast low-molecular-weight ribosomal ribonucleic acid in spinach. Eur J Biochem. 1979 May 15;96(2):311–320. doi: 10.1111/j.1432-1033.1979.tb13042.x. [DOI] [PubMed] [Google Scholar]
  143. Harvey R. J. Growth and initiation of protein synthesis in Escherichia coli in the presence of trimethoprim. J Bacteriol. 1973 Apr;114(1):309–322. doi: 10.1128/jb.114.1.309-322.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  144. Hautala J. A., Bassett C. L., Giles N. H., Kushner S. R. Increased expression of a eukaryotic gene in Escherichia coli through stabilization of its messenger RNA. Proc Natl Acad Sci U S A. 1979 Nov;76(11):5774–5778. doi: 10.1073/pnas.76.11.5774. [DOI] [PMC free article] [PubMed] [Google Scholar]
  145. Held W. A., Gette W. R., Nomura M. Role of 16S ribosomal ribonucleic acid and the 30S ribosomal protein S12 in the initiation of natural messenger ribonucleic acid translation. Biochemistry. 1974 May 7;13(10):2115–2122. doi: 10.1021/bi00707a019. [DOI] [PubMed] [Google Scholar]
  146. Helser T. L., Davies J. E., Dahlberg J. E. Change in methylation of 16S ribosomal RNA associated with mutation to kasugamycin resistance in Escherichia coli. Nat New Biol. 1971 Sep 1;233(35):12–14. doi: 10.1038/newbio233012a0. [DOI] [PubMed] [Google Scholar]
  147. Hendy G. N., Kronenberg H. M., Potts J. T., Jr, Rich A. Nucleotide sequence of cloned cDNAs encoding human preproparathyroid hormone. Proc Natl Acad Sci U S A. 1981 Dec;78(12):7365–7369. doi: 10.1073/pnas.78.12.7365. [DOI] [PMC free article] [PubMed] [Google Scholar]
  148. Hennighausen L. G., Sippel A. E., Hobbs A. A., Rosen J. M. Comparative sequence analysis of the mRNAs coding for mouse and rat whey protein. Nucleic Acids Res. 1982 Jun 25;10(12):3733–3744. doi: 10.1093/nar/10.12.3733. [DOI] [PMC free article] [PubMed] [Google Scholar]
  149. Herring S. W., Sadnik I., Moldave K. Studies on the mechanism of action of a eukaryotic codon-dependent factor specific for initiator Met-tRNAf and ribosomal 40 S subunits. J Biol Chem. 1982 May 10;257(9):4882–4887. [PubMed] [Google Scholar]
  150. Heywood S. M., Kennedy D. S. Messenger RNA affinity column fractionation of eukaryotic initiation factor and the translation of myosin messenger RNA. Arch Biochem Biophys. 1979 Jan;192(1):270–281. doi: 10.1016/0003-9861(79)90092-4. [DOI] [PubMed] [Google Scholar]
  151. Hickey E. D., Weber L. A. Modulation of heat-shock polypeptide synthesis in HeLa cells during hyperthermia and recovery. Biochemistry. 1982 Mar 30;21(7):1513–1521. doi: 10.1021/bi00536a008. [DOI] [PubMed] [Google Scholar]
  152. Higo K., Otaka E., Osawa S. Purification and characterization of 30S ribosomal proteins from Bacillus subtilis: correlation to Escherichia coli 30S proteins. Mol Gen Genet. 1982;185(2):239–244. doi: 10.1007/BF00330792. [DOI] [PubMed] [Google Scholar]
  153. Holland J. P., Holland M. J. The primary structure of a glyceraldehyde-3-phosphate dehydrogenase gene from Saccharomyces cerevisiae. J Biol Chem. 1979 Oct 10;254(19):9839–9845. [PubMed] [Google Scholar]
  154. Holmgren R., Corces V., Morimoto R., Blackman R., Meselson M. Sequence homologies in the 5' regions of four Drosophila heat-shock genes. Proc Natl Acad Sci U S A. 1981 Jun;78(6):3775–3778. doi: 10.1073/pnas.78.6.3775. [DOI] [PMC free article] [PubMed] [Google Scholar]
  155. Horinouchi S., Weisblum B. Posttranscriptional modification of mRNA conformation: mechanism that regulates erythromycin-induced resistance. Proc Natl Acad Sci U S A. 1980 Dec;77(12):7079–7083. doi: 10.1073/pnas.77.12.7079. [DOI] [PMC free article] [PubMed] [Google Scholar]
  156. Horwich A., Koop A. H., Eckhart W. Syntheses and stabilities of proteins related to the polyoma small T antigen in Escherichia coli. Mol Cell Biol. 1982 Jan;2(1):88–92. doi: 10.1128/mcb.2.1.88. [DOI] [PMC free article] [PubMed] [Google Scholar]
  157. Housman D., Jacobs-Lorena M., Rajbhandary U. L., Lodish H. F. Initiation of haemoglobin synthesis by methionyl-tRNA. Nature. 1970 Aug 29;227(5261):913–918. doi: 10.1038/227913a0. [DOI] [PubMed] [Google Scholar]
  158. Howard G. A., Smith R. L., Gordon J. Chicken liver ribosomes: characterization of cross-reaction and inhibition of some functions by antibodies prepared against Escherichia coli ribosomal proteins L7 and L12. J Mol Biol. 1976 Sep 25;106(3):623–637. doi: 10.1016/0022-2836(76)90255-2. [DOI] [PubMed] [Google Scholar]
  159. Hruby D. E., Ball L. A. Mapping and identification of the vaccinia virus thymidine kinase gene. J Virol. 1982 Aug;43(2):403–409. doi: 10.1128/jvi.43.2.403-409.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  160. Huez G., Bruck C., Cleuter Y. Translational stability of native and deadenylylated rabbit globin mRNA injected into HeLa cells. Proc Natl Acad Sci U S A. 1981 Feb;78(2):908–911. doi: 10.1073/pnas.78.2.908. [DOI] [PMC free article] [PubMed] [Google Scholar]
  161. Huez G., Marbaix G., Gallwitz D., Weinberg E., Devos R., Hubert E., Cleuter Y. Functional stabilisation of HeLa cell histone messenger RNAs injected into Xenopus oocytes by 3'-OH polyadenylation. Nature. 1978 Feb 9;271(5645):572–573. doi: 10.1038/271572a0. [DOI] [PubMed] [Google Scholar]
  162. Hunter A. R., Jackson R. J., Hunt T. The role of complexes between the 40-S ribosomal subunit and Met-tRNA-Met-f in the initiation of protein synthesis in the wheat-germ system. Eur J Biochem. 1977 May 2;75(1):159–170. doi: 10.1111/j.1432-1033.1977.tb11513.x. [DOI] [PubMed] [Google Scholar]
  163. Hunter T. R., Hunt T., Knowland J., Zimmern D. Messenger RNA for the coat protein of tobacco mosaic virus. Nature. 1976 Apr 29;260(5554):759–764. doi: 10.1038/260759a0. [DOI] [PubMed] [Google Scholar]
  164. Hörlein D., McPherson J., Goh S. H., Bornstein P. Regulation of protein synthesis: translational control by procollagen-derived fragments. Proc Natl Acad Sci U S A. 1981 Oct;78(10):6163–6167. doi: 10.1073/pnas.78.10.6163. [DOI] [PMC free article] [PubMed] [Google Scholar]
  165. Ikemura T. Correlation between the abundance of yeast transfer RNAs and the occurrence of the respective codons in protein genes. Differences in synonymous codon choice patterns of yeast and Escherichia coli with reference to the abundance of isoaccepting transfer RNAs. J Mol Biol. 1982 Jul 15;158(4):573–597. doi: 10.1016/0022-2836(82)90250-9. [DOI] [PubMed] [Google Scholar]
  166. Ingolia T. D., Craig E. A., McCarthy B. J. Sequence of three copies of the gene for the major Drosophila heat shock induced protein and their flanking regions. Cell. 1980 Oct;21(3):669–679. doi: 10.1016/0092-8674(80)90430-4. [DOI] [PubMed] [Google Scholar]
  167. Ingolia T. D., Craig E. A. Primary sequence of the 5' flanking regions of the Drosophila heat shock genes in chromosome subdivision 67B. Nucleic Acids Res. 1981 Apr 10;9(7):1627–1642. doi: 10.1093/nar/9.7.1627. [DOI] [PMC free article] [PubMed] [Google Scholar]
  168. Isono S., Isono K. Role of ribosomal protein S1 in portein synthesis: effects of its addition to Bacillus stearothermophilus cell-free system. Eur J Biochem. 1975 Aug 1;56(1):15–22. doi: 10.1111/j.1432-1033.1975.tb02202.x. [DOI] [PubMed] [Google Scholar]
  169. Jackson R., Hunter T. Role of methionine in the initiation of haemoglobin synthesis. Nature. 1970 Aug 15;227(5259):672–676. doi: 10.1038/227672a0. [DOI] [PubMed] [Google Scholar]
  170. Jacq B. Sequence homologies between eukaryotic 5.8S rRNA and the 5' end of prokaryotic 23S rRNa: evidences for a common evolutionary origin. Nucleic Acids Res. 1981 Jun 25;9(12):2913–2932. doi: 10.1093/nar/9.12.2913. [DOI] [PMC free article] [PubMed] [Google Scholar]
  171. Jagodzinski L. L., Sargent T. D., Yang M., Glackin C., Bonner J. Sequence homology between RNAs encoding rat alpha-fetoprotein and rat serum albumin. Proc Natl Acad Sci U S A. 1981 Jun;78(6):3521–3525. doi: 10.1073/pnas.78.6.3521. [DOI] [PMC free article] [PubMed] [Google Scholar]
  172. Jagus R., Anderson W. F., Safer B. The regulation of initiation of mammalian protein synthesis. Prog Nucleic Acid Res Mol Biol. 1981;25:127–185. doi: 10.1016/s0079-6603(08)60484-5. [DOI] [PubMed] [Google Scholar]
  173. Jay E., Seth A. K., Jay G. Specific binding of a chemically synthesized prokaryotic ribosome recognition site. Prospect for molecular cloning and expression of eukaryotic genes. J Biol Chem. 1980 May 10;255(9):3809–3812. [PubMed] [Google Scholar]
  174. Jay G., Kaempfer R. Initiation of protein synthesis. Binding of messenger RNA. J Biol Chem. 1975 Aug 10;250(15):5742–5748. [PubMed] [Google Scholar]
  175. Jay G., Khoury G., Seth A. K., Jay E. Construction of a general vector for efficient expression of mammalian proteins in bacteria: use of a synthetic ribosome binding site. Proc Natl Acad Sci U S A. 1981 Sep;78(9):5543–5548. doi: 10.1073/pnas.78.9.5543. [DOI] [PMC free article] [PubMed] [Google Scholar]
  176. Jay G., Nomura S., Anderson C. W., Khoury G. Identification of the SV40 agnogene product: a DNA binding protein. Nature. 1981 May 28;291(5813):346–349. doi: 10.1038/291346a0. [DOI] [PubMed] [Google Scholar]
  177. Jeffreys A. J., Barrie P. A., Harris S., Fawcett D. H., Nugent Z. J., Boyd A. C. Isolation and sequence analysis of a hybrid delta-globin pseudogene from the brown lemur. J Mol Biol. 1982 Apr 15;156(3):487–503. doi: 10.1016/0022-2836(82)90262-5. [DOI] [PubMed] [Google Scholar]
  178. Johnsen M., Christensen T., Dennis P. P., Fiil N. P. Autogenous control: ribosomal protein L10-L12 complex binds to the leader sequence of its mRNA. EMBO J. 1982;1(8):999–1004. doi: 10.1002/j.1460-2075.1982.tb01284.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  179. Johnson B., Szekely M. The binding site of IF-3 in MS2 RNA. Methods Enzymol. 1979;60:343–350. doi: 10.1016/s0076-6879(79)60032-0. [DOI] [PubMed] [Google Scholar]
  180. Johnston H. M., Roth J. R. DNA sequence changes of mutations altering attenuation control of the histidine operon of Salmonella typhimurium. J Mol Biol. 1981 Feb 5;145(4):735–756. doi: 10.1016/0022-2836(81)90312-0. [DOI] [PubMed] [Google Scholar]
  181. Jones C. W., Kafatos F. C. Structure, organization and evolution of developmentally regulated chorion genes in a silkmoth. Cell. 1980 Dec;22(3):855–867. doi: 10.1016/0092-8674(80)90562-0. [DOI] [PubMed] [Google Scholar]
  182. Jones R. L., Sadnik I., Thompson H. A., Moldave K. Studies on native ribosomal subunits from rat liver. Evidence for a low molecular weight ribosome dissociation factor. Arch Biochem Biophys. 1980 Jan;199(1):277–285. doi: 10.1016/0003-9861(80)90282-9. [DOI] [PubMed] [Google Scholar]
  183. Kabat D., Chappell M. R. Competition between globin messenger ribonucleic acids for a discriminating initiation factor. J Biol Chem. 1977 Apr 25;252(8):2684–2690. [PubMed] [Google Scholar]
  184. Kaehler M., Coward J., Rottman F. Cytoplasmic location of undermethylated messenger RNA in Novikoff cells. Nucleic Acids Res. 1979 Mar;6(3):1161–1175. doi: 10.1093/nar/6.3.1161. [DOI] [PMC free article] [PubMed] [Google Scholar]
  185. Kaempfer R. Initiation factor IF-3: a specific inhibitor of ribosomal subunit association. J Mol Biol. 1972 Nov 28;71(3):583–598. doi: 10.1016/s0022-2836(72)80025-1. [DOI] [PubMed] [Google Scholar]
  186. Kaempfer R., van Emmelo J., Fiers W. Specific binding of eukaryotic initiation factor 2 to satellite tobacco necrosis virus RNA at a 5'-terminal sequence comprising the ribosome binding site. Proc Natl Acad Sci U S A. 1981 Mar;78(3):1542–1546. doi: 10.1073/pnas.78.3.1542. [DOI] [PMC free article] [PubMed] [Google Scholar]
  187. Kagramanova V. K., Mankin A. S., Baratova L. A., Bogdanov A. A. The 3'-terminal nucleotide sequence of the Halobacterium halobium 16 S rRNA. FEBS Lett. 1982 Jul 19;144(1):177–180. doi: 10.1016/0014-5793(82)80595-4. [DOI] [PubMed] [Google Scholar]
  188. Kahana C., Gidoni D., Canaani D., Groner Y. Simian virus 40 early mRNA's in lytically infected and transformed cells contain six 5'-terminal caps. J Virol. 1981 Jan;37(1):7–16. doi: 10.1128/jvi.37.1.7-16.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  189. Kakidani H., Furutani Y., Takahashi H., Noda M., Morimoto Y., Hirose T., Asai M., Inayama S., Nakanishi S., Numa S. Cloning and sequence analysis of cDNA for porcine beta-neo-endorphin/dynorphin precursor. Nature. 1982 Jul 15;298(5871):245–249. doi: 10.1038/298245a0. [DOI] [PubMed] [Google Scholar]
  190. Kamen R. I., Wheeler T., Smith A. E. Polyoma virus high molecular weight nuclear RNA codes for capsid protein VP2 in vitro. Virology. 1978 Sep;89(2):461–474. doi: 10.1016/0042-6822(78)90188-5. [DOI] [PubMed] [Google Scholar]
  191. Karam J., Gold L., Singer B. S., Dawson M. Translational regulation: identification of the site on bacteriophage T4 rIIB mRNA recognized by the regA gene function. Proc Natl Acad Sci U S A. 1981 Aug;78(8):4669–4673. doi: 10.1073/pnas.78.8.4669. [DOI] [PMC free article] [PubMed] [Google Scholar]
  192. Karin M., Richards R. I. Human metallothionein genes: molecular cloning and sequence analysis of the mRNA. Nucleic Acids Res. 1982 May 25;10(10):3165–3173. doi: 10.1093/nar/10.10.3165. [DOI] [PMC free article] [PubMed] [Google Scholar]
  193. Kassavetis G. A., Geiduschek E. P. Bacteriophage T4 late promoters: mapping 5' ends of T4 gene 23 mRNAs. EMBO J. 1982;1(1):107–114. doi: 10.1002/j.1460-2075.1982.tb01132.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  194. Kastelein R. A., Remaut E., Fiers W., van Duin J. Lysis gene expression of RNA phage MS2 depends on a frameshift during translation of the overlapping coat protein gene. Nature. 1982 Jan 7;295(5844):35–41. doi: 10.1038/295035a0. [DOI] [PubMed] [Google Scholar]
  195. Keesey J. K., Jr, Bigelis R., Fink G. R. The product of the his4 gene cluster in Saccharomyces cerevisiae. A trifunctional polypeptide. J Biol Chem. 1979 Aug 10;254(15):7427–7433. [PubMed] [Google Scholar]
  196. Kelley D. E., Coleclough C., Perry R. P. Functional significance and evolutionary development of the 5'-terminal regions of immunoglobulin variable-region genes. Cell. 1982 Jun;29(2):681–689. doi: 10.1016/0092-8674(82)90184-2. [DOI] [PubMed] [Google Scholar]
  197. Kemp D. J., Cowman A. F. Direct immunoassay for detecting Escherichia coli colonies that contain polypeptides encoded by cloned DNA segments. Proc Natl Acad Sci U S A. 1981 Jul;78(7):4520–4524. doi: 10.1073/pnas.78.7.4520. [DOI] [PMC free article] [PubMed] [Google Scholar]
  198. Kessel M., Klink F. Archaebacterial elongation factor is ADP-ribosylated by diphtheria toxin. Nature. 1980 Sep 18;287(5779):250–251. doi: 10.1038/287250a0. [DOI] [PubMed] [Google Scholar]
  199. Kikuchi Y., Yoda K., Yamasaki M., Tamura G. The nucleotide sequence of the promoter and the amino-terminal region of alkaline phosphatase structural gene (phoA) of Escherichia coli. Nucleic Acids Res. 1981 Nov 11;9(21):5671–5678. doi: 10.1093/nar/9.21.5671. [DOI] [PMC free article] [PubMed] [Google Scholar]
  200. Kit S., Otsuka H., Qavi H., Kit M. Functional expression of the Herpes simplex virus thymidine kinase gene in Escherichia coli K-12. Gene. 1981 Dec;16(1-3):287–295. doi: 10.1016/0378-1119(81)90084-6. [DOI] [PubMed] [Google Scholar]
  201. Kitamura N., Semler B. L., Rothberg P. G., Larsen G. R., Adler C. J., Dorner A. J., Emini E. A., Hanecak R., Lee J. J., van der Werf S. Primary structure, gene organization and polypeptide expression of poliovirus RNA. Nature. 1981 Jun 18;291(5816):547–553. doi: 10.1038/291547a0. [DOI] [PubMed] [Google Scholar]
  202. Klein W. H., Nolan C., Lazar J. M., Clark J. M., Jr Translation of satellite tobacco necrosis virus ribonucleic acid. I. Characterization of in vitro procaryotic and eucaryotic translation products. Biochemistry. 1972 May 23;11(11):2009–2014. doi: 10.1021/bi00761a003. [DOI] [PubMed] [Google Scholar]
  203. Koch W., Edwards K., Kössel H. Sequencing of the 16S-23S spacer in a ribosomal RNA operon of Zea mays chloroplast DNA reveals two split tRNA genes. Cell. 1981 Jul;25(1):203–213. doi: 10.1016/0092-8674(81)90245-2. [DOI] [PubMed] [Google Scholar]
  204. Konarska M., Filipowicz W., Domdey H., Gross H. J. Binding of ribosomes to linear and circular forms of the 5'-terminal leader fragment of tobacco-mosaic-virus RNA. Eur J Biochem. 1981 Feb;114(2):221–227. doi: 10.1111/j.1432-1033.1981.tb05139.x. [DOI] [PubMed] [Google Scholar]
  205. Kozak M. Analysis of ribosome binding sites from the s1 message of reovirus. Initiation at the first and second AUG codons. J Mol Biol. 1982 Apr 25;156(4):807–820. doi: 10.1016/0022-2836(82)90143-7. [DOI] [PubMed] [Google Scholar]
  206. Kozak M. Evaluation of the "scanning model" for initiation of protein synthesis in eucaryotes. Cell. 1980 Nov;22(1 Pt 1):7–8. doi: 10.1016/0092-8674(80)90148-8. [DOI] [PubMed] [Google Scholar]
  207. Kozak M. How do eucaryotic ribosomes select initiation regions in messenger RNA? Cell. 1978 Dec;15(4):1109–1123. doi: 10.1016/0092-8674(78)90039-9. [DOI] [PubMed] [Google Scholar]
  208. Kozak M. How do eukaryotic ribosomes recognize the unique AUG initiator codon in messenger RNA? Biochem Soc Symp. 1982;47:113–128. [PubMed] [Google Scholar]
  209. Kozak M. Inability of circular mRNA to attach to eukaryotic ribosomes. Nature. 1979 Jul 5;280(5717):82–85. doi: 10.1038/280082a0. [DOI] [PubMed] [Google Scholar]
  210. Kozak M. Influence of mRNA secondary structure on binding and migration of 40S ribosomal subunits. Cell. 1980 Jan;19(1):79–90. doi: 10.1016/0092-8674(80)90390-6. [DOI] [PubMed] [Google Scholar]
  211. Kozak M. Mechanism of mRNA recognition by eukaryotic ribosomes during initiation of protein synthesis. Curr Top Microbiol Immunol. 1981;93:81–123. doi: 10.1007/978-3-642-68123-3_5. [DOI] [PubMed] [Google Scholar]
  212. Kozak M., Nathans D. Translation of the genome of a ribonucleic acid bacteriophage. Bacteriol Rev. 1972 Mar;36(1):109–134. doi: 10.1128/br.36.1.109-134.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  213. Kozak M. Possible role of flanking nucleotides in recognition of the AUG initiator codon by eukaryotic ribosomes. Nucleic Acids Res. 1981 Oct 24;9(20):5233–5252. doi: 10.1093/nar/9.20.5233. [DOI] [PMC free article] [PubMed] [Google Scholar]
  214. Kozak M. Role of ATP in binding and migration of 40S ribosomal subunits. Cell. 1980 Nov;22(2 Pt 2):459–467. doi: 10.1016/0092-8674(80)90356-6. [DOI] [PubMed] [Google Scholar]
  215. Kozak M., Shatkin A. J. Sequences and properties of two ribosome binding sites from the small size class of reovirus messenger RNA. J Biol Chem. 1977 Oct 10;252(19):6895–6908. [PubMed] [Google Scholar]
  216. Krebbers E. T., Larrinua I. M., McIntosh L., Bogorad L. The maize chloroplast genes for the beta and epsilon subunits of the photosynthetic coupling factor CF1 are fused. Nucleic Acids Res. 1982 Aug 25;10(16):4985–5002. doi: 10.1093/nar/10.16.4985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  217. Krisch H. M., Allet B. Nucleotide sequences involved in bacteriophage T4 gene 32 translational self-regulation. Proc Natl Acad Sci U S A. 1982 Aug;79(16):4937–4941. doi: 10.1073/pnas.79.16.4937. [DOI] [PMC free article] [PubMed] [Google Scholar]
  218. Kronenberg M. N., Roberts B. E., Efstratiadis A. The 3' noncoding region of beta-globin mRNA is not essential for in vitro translation. Nucleic Acids Res. 1979 Jan;6(1):153–166. doi: 10.1093/nar/6.1.153. [DOI] [PMC free article] [PubMed] [Google Scholar]
  219. Krug M., de Haseth P. L., Uhlenbeck O. C. Enzymatic synthesis of a 21-nucleotide coat protein binding fragment of R17 ribonucleic acid. Biochemistry. 1982 Sep 14;21(19):4713–4720. doi: 10.1021/bi00262a030. [DOI] [PubMed] [Google Scholar]
  220. Kruiswijk T., Planta R. J. Further analysis of the protein composition of yeast ribosomes. FEBS Lett. 1975 Oct 15;58(1):102–105. doi: 10.1016/0014-5793(75)80235-3. [DOI] [PubMed] [Google Scholar]
  221. Kuchino Y., Ihara M., Yabusaki Y., Nishimura S. Initiator tRNAs from archaebacteria show common unique sequence characteristics. Nature. 1982 Aug 12;298(5875):684–685. doi: 10.1038/298684a0. [DOI] [PubMed] [Google Scholar]
  222. Kuchino Y., Mita T., Nishimura S. Nucleotide sequence of cytoplasmic initiator tRNA from Tetrahymena thermophila. Nucleic Acids Res. 1981 Sep 25;9(18):4557–4562. doi: 10.1093/nar/9.18.4557. [DOI] [PMC free article] [PubMed] [Google Scholar]
  223. Kuebbing D., Liarakos C. D. Nucleotide sequence at the 5' end of ovalbumin messenger RNA from chicken. Nucleic Acids Res. 1978 Jul;5(7):2253–2266. doi: 10.1093/nar/5.7.2253. [DOI] [PMC free article] [PubMed] [Google Scholar]
  224. Kung H. F., Eskin B., Redfield B., Weissbach H. DNA-directed in vitro synthesis of beta-galactosidase: requirement for formylation of methionyl-tRNAf. Arch Biochem Biophys. 1979 Jul;195(2):396–400. doi: 10.1016/0003-9861(79)90366-7. [DOI] [PubMed] [Google Scholar]
  225. Köchel H. G., Küntzel H. Mitochondrial L-rRNA from Aspergillus nidulans: potential secondary structure and evolution. Nucleic Acids Res. 1982 Aug 11;10(15):4795–4801. doi: 10.1093/nar/10.15.4795. [DOI] [PMC free article] [PubMed] [Google Scholar]
  226. Lambowitz A. M., Chua N. H., Luck D. J. Mitochondrial ribosome assembly in Neurospora. Preparation of mitochondrial ribosomal precursor particles, site of synthesis of mitochondrial ribosomal proteins and studies on the poky mutant. J Mol Biol. 1976 Nov 5;107(3):223–253. doi: 10.1016/s0022-2836(76)80003-4. [DOI] [PubMed] [Google Scholar]
  227. Lang-Yang H., Zubay G. Negative regulation of beta and beta' synthesis by RNA polymerase. Mol Gen Genet. 1981;183(3):514–517. doi: 10.1007/BF00268773. [DOI] [PubMed] [Google Scholar]
  228. Lawn R. M., Adelman J., Bock S. C., Franke A. E., Houck C. M., Najarian R. C., Seeburg P. H., Wion K. L. The sequence of human serum albumin cDNA and its expression in E. coli. Nucleic Acids Res. 1981 Nov 25;9(22):6103–6114. doi: 10.1093/nar/9.22.6103. [DOI] [PMC free article] [PubMed] [Google Scholar]
  229. Lebowitz P., Weissman S. M. Organization and transcription of the simian virus 40 genome. Curr Top Microbiol Immunol. 1979;87:43–172. doi: 10.1007/978-3-642-67344-3_3. [DOI] [PubMed] [Google Scholar]
  230. Lee S. G., Evans W. R. Hybrid ribosome formation from Escherichia coli and chloroplast ribosome subunits. Science. 1971 Jul 16;173(3993):241–242. doi: 10.1126/science.173.3993.241. [DOI] [PubMed] [Google Scholar]
  231. Legon S., Model P., Robertson H. D. Interaction of rabbit reticulocyte ribosomes with bacteriophage f1 mRNA and of Escherichia coli ribosomes with rabbit globin mRNA. Proc Natl Acad Sci U S A. 1977 Jul;74(7):2692–2696. doi: 10.1073/pnas.74.7.2692. [DOI] [PMC free article] [PubMed] [Google Scholar]
  232. Legon S. The binding of ribosomes to polyoma virus RNA. Possible role of the leader region in initiation site recognition. J Mol Biol. 1979 Oct 25;134(2):219–240. doi: 10.1016/0022-2836(79)90033-0. [DOI] [PubMed] [Google Scholar]
  233. Lemaire G., Gold L., Yarus M. Autogenous translational repression of bacteriophage T4 gene 32 expression in vitro. J Mol Biol. 1978 Nov 25;126(1):73–90. doi: 10.1016/0022-2836(78)90280-2. [DOI] [PubMed] [Google Scholar]
  234. Levens D., Ticho B., Ackerman E., Rabinowitz M. Transcriptional initiation and 5' termini of yeast mitochondrial RNA. J Biol Chem. 1981 May 25;256(10):5226–5232. [PubMed] [Google Scholar]
  235. Lewin B. Alternatives for splicing: an intron-coded protein. Cell. 1980 Dec;22(3):645–646. doi: 10.1016/0092-8674(80)90538-3. [DOI] [PubMed] [Google Scholar]
  236. Lewin B. Alternatives for splicing: recognizing the ends of introns. Cell. 1980 Nov;22(2 Pt 2):324–326. doi: 10.1016/0092-8674(80)90340-2. [DOI] [PubMed] [Google Scholar]
  237. Li M., Tzagoloff A., Underbrink-Lyon K., Martin N. C. Identification of the paromomycin-resistance mutation in the 15 S rRNA gene of yeast mitochondria. J Biol Chem. 1982 May 25;257(10):5921–5928. [PubMed] [Google Scholar]
  238. Lin A., Wittmann-Liebold B., McNally J., Wool I. G. The primary structure of the acidic phosphoprotein P2 from rat liver 60 S ribosomal subunits. Comparison with ribosomal 'A' proteins from other species. J Biol Chem. 1982 Aug 10;257(15):9189–9197. [PubMed] [Google Scholar]
  239. Lingappa V. R., Cunningham B. A., Jazwinski S. M., Hopp T. P., Blobel G., Edelman G. M. Cell-free synthesis and segregation of beta 2-microglobulin. Proc Natl Acad Sci U S A. 1979 Aug;76(8):3651–3655. doi: 10.1073/pnas.76.8.3651. [DOI] [PMC free article] [PubMed] [Google Scholar]
  240. Lockard R. E., Connaughton J. F., Kumar A. Nucleotide sequence of the 5'- and 3'- domains for rabbit 18S ribosomal RNA. Nucleic Acids Res. 1982 Jun 11;10(11):3445–3457. doi: 10.1093/nar/10.11.3445. [DOI] [PMC free article] [PubMed] [Google Scholar]
  241. Lodish H. F., Rose J. K. Relative importance of 7-methylguanosine in ribosome binding and translation of vesicular stomatitis virus mRNA in wheat germ and reticulocyte cell-free systems. J Biol Chem. 1977 Feb 25;252(4):1181–1188. [PubMed] [Google Scholar]
  242. Lodish H. F. Secondary structure of bacteriophage f2 ribonucleic acid and the initiation of in vitro protein biosynthesis. J Mol Biol. 1970 Jun 28;50(3):689–702. doi: 10.1016/0022-2836(70)90093-8. [DOI] [PubMed] [Google Scholar]
  243. Lodish H. F. Species specificity of polypeptide chain initiation. Nature. 1969 Nov 29;224(5222):867–870. doi: 10.1038/224867a0. [DOI] [PubMed] [Google Scholar]
  244. Lodish H. F. Specificity in bacterial protein synthesis: role of initiation factors and ribosomal subunits. Nature. 1970 May 23;226(5247):705–707. doi: 10.1038/226705a0. [DOI] [PubMed] [Google Scholar]
  245. Lomedico P. T., McAndrew S. J. Eukaryotic ribosomes can recognize preproinsulin initiation codons irrespective of their position relative to the 5' end of mRNA. Nature. 1982 Sep 16;299(5880):221–226. doi: 10.1038/299221a0. [DOI] [PubMed] [Google Scholar]
  246. Long E. O., Dawid I. B. Repeated genes in eukaryotes. Annu Rev Biochem. 1980;49:727–764. doi: 10.1146/annurev.bi.49.070180.003455. [DOI] [PubMed] [Google Scholar]
  247. Loughney K., Lund E., Dahlberg J. E. tRNA genes are found between 16S and 23S rRNA genes in Bacillus subtilis. Nucleic Acids Res. 1982 Mar 11;10(5):1607–1624. doi: 10.1093/nar/10.5.1607. [DOI] [PMC free article] [PubMed] [Google Scholar]
  248. Lucchini G., Bianchetti R. Initiation of protein synthesis in isolated mitochondria and chloroplasts. Biochim Biophys Acta. 1980 Jun 27;608(1):54–61. doi: 10.1016/0005-2787(80)90133-1. [DOI] [PubMed] [Google Scholar]
  249. Lundquist R. E., Lazar J. M., Klein W. H., Clark J. M., Jr Translation of satellite tobacco necrosis virus ribonucleic acid. II. Initiation of in vitro translation in procaryotic and eucaryotic systems. Biochemistry. 1972 May 23;11(11):2014–2019. doi: 10.1021/bi00761a004. [DOI] [PubMed] [Google Scholar]
  250. Lynch D. C., Attardi G. Amino acid specificity of the transfer RNA species coded for by HeLa cell mitochondrial DNA. J Mol Biol. 1976 Mar 25;102(1):125–141. doi: 10.1016/0022-2836(76)90077-2. [DOI] [PubMed] [Google Scholar]
  251. MacDonald R. J., Stary S. J., Swift G. H. Two similar but nonallelic rat pancreatic trypsinogens. Nucleotide sequences of the cloned cDNAs. J Biol Chem. 1982 Aug 25;257(16):9724–9732. [PubMed] [Google Scholar]
  252. MacDonald R. J., Swift G. H., Quinto C., Swain W., Pictet R. L., Nikovits W., Rutter W. J. Primary structure of two distinct rat pancreatic preproelastases determined by sequence analysis of the complete cloned messenger ribonucleic acid sequences. Biochemistry. 1982 Mar 16;21(6):1453–1463. doi: 10.1021/bi00535a053. [DOI] [PubMed] [Google Scholar]
  253. Machatt M. A., Ebel J. P., Branlant C. The 3'-terminal region of bacterial 23S ribosomal RNA: structure and homology with the 3'-terminal region of eukaryotic 28S rRNA and with chloroplast 4.5s rRNA. Nucleic Acids Res. 1981 Apr 10;9(7):1533–1549. doi: 10.1093/nar/9.7.1533. [DOI] [PMC free article] [PubMed] [Google Scholar]
  254. Macino G., Tzagoloff A. Assembly of the mitochondrial membrane system. The DNA sequence of a mitochondrial ATPase gene in Saccharomyces cerevisiae. J Biol Chem. 1979 Jun 10;254(11):4617–4623. [PubMed] [Google Scholar]
  255. Mackie G. A. Nucleotide sequence of the gene for ribosomal protein S20 and its flanking regions. J Biol Chem. 1981 Aug 10;256(15):8177–8182. [PubMed] [Google Scholar]
  256. Maitra U., Stringer E. A., Chaudhuri A. Initiation factors in protein biosynthesis. Annu Rev Biochem. 1982;51:869–900. doi: 10.1146/annurev.bi.51.070182.004253. [DOI] [PubMed] [Google Scholar]
  257. Manley J. L. Synthesis of internal re-initiation fragments of beta-galactosidase in vitro and in vivo. J Mol Biol. 1978 Nov 15;125(4):449–466. doi: 10.1016/0022-2836(78)90310-8. [DOI] [PubMed] [Google Scholar]
  258. Marcus A. Tobacco mosaic virus ribonucleic acid-dependent amino acid incorporation in a wheat embryo system in vitro. Formation of a ribosome-messenger "initiation" complex. J Biol Chem. 1970 Mar 10;245(5):962–966. [PubMed] [Google Scholar]
  259. Martin N. C., rabinowitz M. Mitochondrial transfer RNAs in yeast: identification of isoaccepting transfer RNAs. Biochemistry. 1978 May 2;17(9):1628–1634. doi: 10.1021/bi00602a008. [DOI] [PubMed] [Google Scholar]
  260. Martin S. L., Zimmer E. A., Davidson W. S., Wilson A. C., Kan Y. W. The untranslated regions of beta-globin mRNA evolve at a functional rate in higher primates. Cell. 1981 Sep;25(3):737–741. doi: 10.1016/0092-8674(81)90181-1. [DOI] [PubMed] [Google Scholar]
  261. Matthews D. E., Hessler R. A., Denslow N. D., Edwards J. S., O'Brien T. W. Protein composition of the bovine mitochondrial ribosome. J Biol Chem. 1982 Aug 10;257(15):8788–8794. [PubMed] [Google Scholar]
  262. Mattick J. S., Zehner Z. E., Calabro M. A., Wakil S. J. The isolation and characterization of fatty-acid synthetase mRNA from rat mammary gland. Eur J Biochem. 1981 Mar;114(3):643–651. doi: 10.1111/j.1432-1033.1981.tb05192.x. [DOI] [PubMed] [Google Scholar]
  263. McKeown M., Firtel R. A. Differential expression and 5' end mapping of actin genes in Dictyostelium. Cell. 1981 Jun;24(3):799–807. doi: 10.1016/0092-8674(81)90105-7. [DOI] [PubMed] [Google Scholar]
  264. McLaughlin J. R., Chang S. Y., Chang S. Transcriptional analyses of the Bacillus licheniformis penP gene. Nucleic Acids Res. 1982 Jul 10;10(13):3905–3919. doi: 10.1093/nar/10.13.3905. [DOI] [PMC free article] [PubMed] [Google Scholar]
  265. McLaughlin J. R., Murray C. L., Rabinowitz J. C. Unique features in the ribosome binding site sequence of the gram-positive Staphylococcus aureus beta-lactamase gene. J Biol Chem. 1981 Nov 10;256(21):11283–11291. [PubMed] [Google Scholar]
  266. Meagher R. B., Tait R. C., Betlach M., Boyer H. W. Protein expression in E. coli minicells by recombinant plasmids. Cell. 1977 Mar;10(3):521–536. doi: 10.1016/0092-8674(77)90039-3. [DOI] [PubMed] [Google Scholar]
  267. Meijlink F. C., van het Schip A. D., Arnberg A. C., Wieringa B., Ab G., Gruber M. Structure of the chicken apo very low density lipoprotein II gene. J Biol Chem. 1981 Sep 25;256(18):9668–9671. [PubMed] [Google Scholar]
  268. Mellado R. P., Delius H., Klein B., Murray K. Transcription of sea urchin histone genes in Escherichia coli. Nucleic Acids Res. 1981 Aug 25;9(16):3889–3906. doi: 10.1093/nar/9.16.3889. [DOI] [PMC free article] [PubMed] [Google Scholar]
  269. Meyer D. I., Krause E., Dobberstein B. Secretory protein translocation across membranes-the role of the "docking protein'. Nature. 1982 Jun 24;297(5868):647–650. doi: 10.1038/297647a0. [DOI] [PubMed] [Google Scholar]
  270. Meyer T. F., Beyreuther K., Geider K. Recognition of two initiation codons for the synthesis of phage fd gene 2 protein. Mol Gen Genet. 1980;180(3):489–494. doi: 10.1007/BF00268051. [DOI] [PubMed] [Google Scholar]
  271. Michelson A. M., Orkin S. H. The 3' untranslated regions of the duplicated human alpha-globin genes are unexpectedly divergent. Cell. 1980 Nov;22(2 Pt 2):371–377. doi: 10.1016/0092-8674(80)90347-5. [DOI] [PubMed] [Google Scholar]
  272. Miyata T., Yasunaga T., Nishida T. Nucleotide sequence divergence and functional constraint in mRNA evolution. Proc Natl Acad Sci U S A. 1980 Dec;77(12):7328–7332. doi: 10.1073/pnas.77.12.7328. [DOI] [PMC free article] [PubMed] [Google Scholar]
  273. Mizushima S., Nomura M. Assembly mapping of 30S ribosomal proteins from E. coli. Nature. 1970 Jun 27;226(5252):1214–1214. doi: 10.1038/2261214a0. [DOI] [PubMed] [Google Scholar]
  274. Model P., McGill C., Mazur B., Fulford W. D. The replication of bacteriophage f1: gene V protein regulates the synthesis of gene II protein. Cell. 1982 Jun;29(2):329–335. doi: 10.1016/0092-8674(82)90149-0. [DOI] [PubMed] [Google Scholar]
  275. Monk R. J., Meyuhas O., Perry R. P. Mammals have multiple genes for individual ribosomal proteins. Cell. 1981 May;24(2):301–306. doi: 10.1016/0092-8674(81)90319-6. [DOI] [PubMed] [Google Scholar]
  276. Montgomery D. L., Leung D. W., Smith M., Shalit P., Faye G., Hall B. D. Isolation and sequence of the gene for iso-2-cytochrome c in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A. 1980 Jan;77(1):541–545. doi: 10.1073/pnas.77.1.541. [DOI] [PMC free article] [PubMed] [Google Scholar]
  277. Montoya J., Ojala D., Attardi G. Distinctive features of the 5'-terminal sequences of the human mitochondrial mRNAs. Nature. 1981 Apr 9;290(5806):465–470. doi: 10.1038/290465a0. [DOI] [PubMed] [Google Scholar]
  278. Moyer S. A. Alteration of the 5' terminal caps of the mRNAs of vesicular stomatitis virus by cycloleucine in vivo. Virology. 1981 Jul 15;112(1):157–168. doi: 10.1016/0042-6822(81)90621-8. [DOI] [PubMed] [Google Scholar]
  279. Mulligan R. C., Berg P. Factors governing the expression of a bacterial gene in mammalian cells. Mol Cell Biol. 1981 May;1(5):449–459. doi: 10.1128/mcb.1.5.449. [DOI] [PMC free article] [PubMed] [Google Scholar]
  280. Murray C. L., Rabinowitz J. C. Nucleotide sequences of transcription and translation initiation regions in Bacillus phage phi 29 early genes. J Biol Chem. 1982 Jan 25;257(2):1053–1062. [PubMed] [Google Scholar]
  281. Muskavitch M. A., Hogness D. S. An expandable gene that encodes a Drosophila glue protein is not expressed in variants lacking remote upstream sequences. Cell. 1982 Jul;29(3):1041–1051. doi: 10.1016/0092-8674(82)90467-6. [DOI] [PubMed] [Google Scholar]
  282. Müller U. R., Wells R. D. Intercistronic regions in phi X174 DNA. II. Biochemical and biological analysis of mutants with altered intercistronic regions between genes J and F. J Mol Biol. 1980 Jul 25;141(1):25–41. doi: 10.1016/s0022-2836(80)80027-1. [DOI] [PubMed] [Google Scholar]
  283. Nakanishi S., Teranishi Y., Noda M., Notake M., Watanabe Y., Kakidani H., Jingami H., Numa S. The protein-coding sequence of the bovine ACTH-beta-LPH precursor gene is split near the signal peptide region. Nature. 1980 Oct 23;287(5784):752–755. doi: 10.1038/287752a0. [DOI] [PubMed] [Google Scholar]
  284. Nakashima K., Darzynkiewicz E., Shatkin A. J. Proximity of mRNA5'-region and 18S rRNA in eukaryotic initiation complexes. Nature. 1980 Jul 17;286(5770):226–230. doi: 10.1038/286226a0. [DOI] [PubMed] [Google Scholar]
  285. Nakazato H., Venkatesan S., Edmonds M. Polyadenylic acid sequences in E. coli messenger RNA. Nature. 1975 Jul 10;256(5513):144–146. doi: 10.1038/256144a0. [DOI] [PubMed] [Google Scholar]
  286. Napoli C., Gold L., Singer B. S. Translational reinitiation in the rIIB cistron of bacteriophage T4. J Mol Biol. 1981 Jul 5;149(3):433–449. doi: 10.1016/0022-2836(81)90480-0. [DOI] [PubMed] [Google Scholar]
  287. Nazar R. N. A 5.8 S rRNA-like sequence in prokaryotic 23 S rRNA. FEBS Lett. 1980 Oct 6;119(2):212–214. doi: 10.1016/0014-5793(80)80254-7. [DOI] [PubMed] [Google Scholar]
  288. Nazar R. N. Evolutionary relationship between eukaryotic 29--32 S nucleolar rRNA precursors and the prokaryotic 23 S rRNA. FEBS Lett. 1982 Jul 5;143(2):161–162. doi: 10.1016/0014-5793(82)80089-6. [DOI] [PubMed] [Google Scholar]
  289. Netzker R., Köchel H. G., Basak N., Küntzel H. Nucleotide sequence of Aspergillus nidulans mitochondrial genes coding for ATPase subunit 6, cytochrome oxidase subunit 3, seven unidentified proteins, four tRNAs and L-rRNA. Nucleic Acids Res. 1982 Aug 11;10(15):4783–4794. doi: 10.1093/nar/10.15.4783. [DOI] [PMC free article] [PubMed] [Google Scholar]
  290. Nguyen-Huu M. C., Stratmann M., Groner B., Wurtz T., Land H., Giesecke K., Sippel A. E., Schütz G. Chicken lysozyme gene contains several intervening sequences. Proc Natl Acad Sci U S A. 1979 Jan;76(1):76–80. doi: 10.1073/pnas.76.1.76. [DOI] [PMC free article] [PubMed] [Google Scholar]
  291. Nichols B. P., van Cleemput M., Yanofsky C. Nucleotide sequence of Escherichia coli trpE. Anthranilate synthetase component I contains no tryptophan residues. J Mol Biol. 1981 Feb 15;146(1):45–54. doi: 10.1016/0022-2836(81)90365-x. [DOI] [PubMed] [Google Scholar]
  292. Nierhaus K. H. Structure, assembly, and function of ribosomes. Curr Top Microbiol Immunol. 1982;97:81–155. doi: 10.1007/978-3-642-68318-3_3. [DOI] [PubMed] [Google Scholar]
  293. Noda M., Teranishi Y., Takahashi H., Toyosato M., Notake M., Nakanishi S., Numa S. Isolation and structural organization of the human preproenkephalin gene. Nature. 1982 Jun 3;297(5865):431–434. doi: 10.1038/297431a0. [DOI] [PubMed] [Google Scholar]
  294. Noll M., Noll H., Lingrel J. B. Initiation factor IF-3-dependent binding of Escherichia coli ribosomes and N-formylmethionine transfer-RNA to rabbit globin messenger. Proc Natl Acad Sci U S A. 1972 Jul;69(7):1843–1847. doi: 10.1073/pnas.69.7.1843. [DOI] [PMC free article] [PubMed] [Google Scholar]
  295. Noller H. F., Woese C. R. Secondary structure of 16S ribosomal RNA. Science. 1981 Apr 24;212(4493):403–411. doi: 10.1126/science.6163215. [DOI] [PubMed] [Google Scholar]
  296. Nomura M., Erdmann V. A. Reconstitution of 50S ribosomal subunits from dissociated molecular components. Nature. 1970 Nov 21;228(5273):744–748. doi: 10.1038/228744a0. [DOI] [PubMed] [Google Scholar]
  297. Nomura M., Morgan E. A. Genetics of bacterial ribosomes. Annu Rev Genet. 1977;11:297–347. doi: 10.1146/annurev.ge.11.120177.001501. [DOI] [PubMed] [Google Scholar]
  298. Nomura M., Yates J. L., Dean D., Post L. E. Feedback regulation of ribosomal protein gene expression in Escherichia coli: structural homology of ribosomal RNA and ribosomal protein MRNA. Proc Natl Acad Sci U S A. 1980 Dec;77(12):7084–7088. doi: 10.1073/pnas.77.12.7084. [DOI] [PMC free article] [PubMed] [Google Scholar]
  299. O'Hare K., Benoist C., Breathnach R. Transformation of mouse fibroblasts to methotrexate resistance by a recombinant plasmid expressing a prokaryotic dihydrofolate reductase. Proc Natl Acad Sci U S A. 1981 Mar;78(3):1527–1531. doi: 10.1073/pnas.78.3.1527. [DOI] [PMC free article] [PubMed] [Google Scholar]
  300. Olins P. O., Jones D. S. Nucleotide sequence of Scenedesmus obliquus cytoplasmic initiator tRNA. Nucleic Acids Res. 1980 Feb 25;8(4):715–729. [PMC free article] [PubMed] [Google Scholar]
  301. Olson H. M., Glitz D. G. Ribosome structure: localization of 3' end of RNA in small subunit by immunoelectronmicroscopy. Proc Natl Acad Sci U S A. 1979 Aug;76(8):3769–3773. doi: 10.1073/pnas.76.8.3769. [DOI] [PMC free article] [PubMed] [Google Scholar]
  302. Orozco E. M., Jr, Rushlow K. E., Dodd J. R., Hallick R. B. Euglena gracilis chloroplast ribosomal RNA transcription units. II. Nucleotide sequence homology between the 16 S--23 S ribosomal RNA spacer and the 16 S ribosomal RNA leader regions. J Biol Chem. 1980 Nov 25;255(22):10997–11003. [PubMed] [Google Scholar]
  303. Osborne T. F., Gaynor R. B., Berk A. J. The TATA homology and the mRNA 5' untranslated sequence are not required for expression of essential adenovirus E1A functions. Cell. 1982 May;29(1):139–148. doi: 10.1016/0092-8674(82)90098-8. [DOI] [PubMed] [Google Scholar]
  304. Ovchinnikov Y. A., Monastyrskaya G. S., Gubanov V. V., Guryev S. O., Chertov OYu, Modyanov N. N., Grinkevich V. A., Makarova I. A., Marchenko T. V., Polovnikova I. N. The primary structure of Escherichia coli RNA polymerase. Nucleotide sequence of the rpoB gene and amino-acid sequence of the beta-subunit. Eur J Biochem. 1981 Jun 1;116(3):621–629. doi: 10.1111/j.1432-1033.1981.tb05381.x. [DOI] [PubMed] [Google Scholar]
  305. Padilla M., Canaani D., Groner Y., Weinstein J. A., Bar-Joseph M., Merrick W., Shafritz D. A. Initiation factor eIF-4B (IF-M3)-dependent recognition and translation of capped versus uncapped eukaryotic mRNAs. J Biol Chem. 1978 Sep 10;253(17):5939–5945. [PubMed] [Google Scholar]
  306. Palmiter R. D., Gagnon J., Ericsson L. H., Walsh K. A. Precursor of egg white lysozyme. Amino acid sequence of an NH2-terminal extension. J Biol Chem. 1977 Sep 25;252(18):6386–6393. [PubMed] [Google Scholar]
  307. Palmiter R. D., Gagnon J., Walsh K. A. Ovalbumin: a secreted protein without a transient hydrophobic leader sequence. Proc Natl Acad Sci U S A. 1978 Jan;75(1):94–98. doi: 10.1073/pnas.75.1.94. [DOI] [PMC free article] [PubMed] [Google Scholar]
  308. Paterson B. M., Rosenberg M. Efficient translation of prokaryotic mRNAs in a eukaryotic cell-free system requires addition of a cap structure. Nature. 1979 Jun 21;279(5715):692–696. doi: 10.1038/279692a0. [DOI] [PubMed] [Google Scholar]
  309. Pauza C. D., Karels M. J., Navre M., Schachman H. K. Genes encoding Escherichia coli aspartate transcarbamoylase: the pyrB-pyrI operon. Proc Natl Acad Sci U S A. 1982 Jul;79(13):4020–4024. doi: 10.1073/pnas.79.13.4020. [DOI] [PMC free article] [PubMed] [Google Scholar]
  310. Pavlakis G. N., Jordan B. R., Wurst R. M., Vournakis J. N. Sequence and secondary structure of Drosophila melanogaster 5.8S and 2S rRNAs and of the processing site between them. Nucleic Acids Res. 1979 Dec 20;7(8):2213–2238. doi: 10.1093/nar/7.8.2213. [DOI] [PMC free article] [PubMed] [Google Scholar]
  311. Peacock S., Cenatiempo Y., Robakis N., Brot N., Weissbach H. In vitro synthesis of the first dipeptide of the beta subunit of Escherichia coli RNA polymerase. Proc Natl Acad Sci U S A. 1982 Aug;79(15):4609–4612. doi: 10.1073/pnas.79.15.4609. [DOI] [PMC free article] [PubMed] [Google Scholar]
  312. Pearson N. J., Fried H. M., Warner J. R. Yeast use translational control to compensate for extra copies of a ribosomal protein gene. Cell. 1982 Jun;29(2):347–355. doi: 10.1016/0092-8674(82)90151-9. [DOI] [PubMed] [Google Scholar]
  313. Perler F., Efstratiadis A., Lomedico P., Gilbert W., Kolodner R., Dodgson J. The evolution of genes: the chicken preproinsulin gene. Cell. 1980 Jun;20(2):555–566. doi: 10.1016/0092-8674(80)90641-8. [DOI] [PubMed] [Google Scholar]
  314. Perry R. P. Processing of RNA. Annu Rev Biochem. 1976;45:605–629. doi: 10.1146/annurev.bi.45.070176.003133. [DOI] [PubMed] [Google Scholar]
  315. Petersen H. U., Røll T., Grunberg-Manago M., Clark B. F. Specific interaction of initiation factor IF2 of E. coli with formylmethionyl-tRNA f Met. Biochem Biophys Res Commun. 1979 Dec 14;91(3):1068–1074. doi: 10.1016/0006-291x(79)91989-2. [DOI] [PubMed] [Google Scholar]
  316. Peterson D. T., Merrick W. C., Safer B. Binding and release of radiolabeled eukaryotic initiation factors 2 and 3 during 80 S initiation complex formation. J Biol Chem. 1979 Apr 10;254(7):2509–2516. [PubMed] [Google Scholar]
  317. Peterson D. T., Safer B., Merrick W. C. Role of eukaryotic initiation factor 5 in the formation of 80 S initiation complexes. J Biol Chem. 1979 Aug 25;254(16):7730–7735. [PubMed] [Google Scholar]
  318. Phillips S. L., Tse C., Serventi I., Hynes N. Structure of polyadenylic acid in the ribonucleic acid of Saccharomyces cerevisiae. J Bacteriol. 1979 May;138(2):542–551. doi: 10.1128/jb.138.2.542-551.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  319. Pinck M., Fritsch C., Ravelonandro M., Thivent C., Pinck L. Binding of ribosomes to the 5' leader sequence (N = 258) of RNA 3 from alfalfa mosaic virus. Nucleic Acids Res. 1981 Mar 11;9(5):1087–1100. doi: 10.1093/nar/9.5.1087. [DOI] [PMC free article] [PubMed] [Google Scholar]
  320. Pirrotta V. Operators and promoters in the OR region of phage 434. Nucleic Acids Res. 1979 Apr;6(4):1495–1508. doi: 10.1093/nar/6.4.1495. [DOI] [PMC free article] [PubMed] [Google Scholar]
  321. Poole S., Firtel R. A., Lamar E., Rowekamp W. Sequence and expression of the discoidin I gene family in Dictyostelium discoideum. J Mol Biol. 1981 Dec 5;153(2):273–289. doi: 10.1016/0022-2836(81)90278-3. [DOI] [PubMed] [Google Scholar]
  322. Porter A. G., Hindley J. The binding of Q initiator fragments to E. coli ribosomes. FEBS Lett. 1973 Jul 15;33(3):339–342. doi: 10.1016/0014-5793(73)80225-x. [DOI] [PubMed] [Google Scholar]
  323. Post L. E., Arfsten A. E., Davis G. R., Nomura M. DNA sequence of the promoter region for the alpha ribosomal protein operon in Escherichia coli. J Biol Chem. 1980 May 25;255(10):4653–4659. [PubMed] [Google Scholar]
  324. Post L. E., Nomura M. DNA sequences from the str operon of Escherichia coli. J Biol Chem. 1980 May 25;255(10):4660–4666. [PubMed] [Google Scholar]
  325. Preston C. M., McGeoch D. J. Identification and mapping of two polypeptides encoded within the herpes simplex virus type 1 thymidine kinase gene sequences. J Virol. 1981 May;38(2):593–605. doi: 10.1128/jvi.38.2.593-605.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  326. Proudfoot N. J., Maniatis T. The structure of a human alpha-globin pseudogene and its relationship to alpha-globin gene duplication. Cell. 1980 Sep;21(2):537–544. doi: 10.1016/0092-8674(80)90491-2. [DOI] [PubMed] [Google Scholar]
  327. Ptashne M., Backman K., Humayun M. Z., Jeffrey A., Maurer R., Meyer B., Sauer R. T. Autoregulation and function of a repressor in bacteriophage lambda. Science. 1976 Oct 8;194(4261):156–161. doi: 10.1126/science.959843. [DOI] [PubMed] [Google Scholar]
  328. Queen C., Rosenberg M. Differential translation efficiency explains discoordinate expression of the galactose operon. Cell. 1981 Jul;25(1):241–249. doi: 10.1016/0092-8674(81)90249-x. [DOI] [PubMed] [Google Scholar]
  329. RajBhandary U. L., Ghosh H. P. Studies on polynucleotides. XCI. Yeast methionine transfer ribonucleic acid: purification, properties, and terminal nucleotide sequences. J Biol Chem. 1969 Mar 10;244(5):1104–1113. [PubMed] [Google Scholar]
  330. Rambach A., Hogness D. S. Translation of Drosophila melanogaster sequences in Escherichia coli. Proc Natl Acad Sci U S A. 1977 Nov;74(11):5041–5045. doi: 10.1073/pnas.74.11.5041. [DOI] [PMC free article] [PubMed] [Google Scholar]
  331. Ramjoué H. P., Gordon J. Evolutionary microdivergence of chick and rat liver ribosomal proteins. J Biol Chem. 1977 Dec 25;252(24):9065–9070. [PubMed] [Google Scholar]
  332. Ranu R. S., Wool I. G. Discrimination between eukaryotic and prokaryotic, and formylated and non-formylated, initiator tRNAs by eukaryotic initiation factor EIF-3. Nature. 1975 Oct 16;257(5527):616–618. doi: 10.1038/257616a0. [DOI] [PubMed] [Google Scholar]
  333. Rekosh D. M., Lodish H., Baltimore D. Protein synthesis in Escherichia coli extracts programmed by poliovirus RNA. J Mol Biol. 1970 Dec 14;54(2):327–340. doi: 10.1016/0022-2836(70)90433-x. [DOI] [PubMed] [Google Scholar]
  334. Remaut E., Waele P. D., Marmenout A., Stanssens P., Fiers W. Functional expression of individual plasmid-coded RNA bacteriophage MS2 genes. EMBO J. 1982;1(2):205–209. doi: 10.1002/j.1460-2075.1982.tb01148.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  335. Richer L. L. The efficiency of methionine incorporation from isoaccepting species of tRNAMet into rabbit globin in an homologous reticulocyte lysate system. Biochim Biophys Acta. 1978 Jan 26;517(1):76–83. doi: 10.1016/0005-2787(78)90035-7. [DOI] [PubMed] [Google Scholar]
  336. Richter D. Production of mitochondrial peptide-chain elongation factors in yeast deficient in mitochondrial deoxyribonucleic acid. Biochemistry. 1971 Nov 23;10(24):4422–4425. doi: 10.1021/bi00800a011. [DOI] [PubMed] [Google Scholar]
  337. Roberts T. M., Bikel I., Yocum R. R., Livingston D. M., Ptashne M. Synthesis of simian virus 40 t antigen in Escherichia coli. Proc Natl Acad Sci U S A. 1979 Nov;76(11):5596–5600. doi: 10.1073/pnas.76.11.5596. [DOI] [PMC free article] [PubMed] [Google Scholar]
  338. Roberts T. M., Kacich R., Ptashne M. A general method for maximizing the expression of a cloned gene. Proc Natl Acad Sci U S A. 1979 Feb;76(2):760–764. doi: 10.1073/pnas.76.2.760. [DOI] [PMC free article] [PubMed] [Google Scholar]
  339. Rochaix J. D., Darlix J. L. Composite structure of the chloroplast 23 S ribosomal RNA genes of Chlamydomonas reinhardii. Evolutionary and functional implications. J Mol Biol. 1982 Aug 15;159(3):383–395. doi: 10.1016/0022-2836(82)90290-x. [DOI] [PubMed] [Google Scholar]
  340. Rosa M. D. Structure analysis of three T7 late mRNA ribosome binding sites. J Mol Biol. 1981 Mar 25;147(1):55–71. doi: 10.1016/0022-2836(81)90079-6. [DOI] [PubMed] [Google Scholar]
  341. Rosenberg M., Paterson B. M. Efficient cap-dependent translation of polycistronic prokaryotic mRNAs is restricted to the first gene in the operon. Nature. 1979 Jun 21;279(5715):696–701. doi: 10.1038/279696a0. [DOI] [PubMed] [Google Scholar]
  342. Rubenstein P., Smith P., Deuchler J., Redman K. NH2-terminal acetylation of Dictyostelium discoideum actin in a cell-free protein-synthesizing system. J Biol Chem. 1981 Aug 10;256(15):8149–8155. [PubMed] [Google Scholar]
  343. Rubtsov P. M., Musakhanov M. M., Zakharyev V. M., Krayev A. S., Skryabin K. G., Bayev A. A. The structure of the yeast ribosomal RNA genes. I. The complete nucleotide sequence of the 18S ribosomal RNA gene from Saccharomyces cerevisiae. Nucleic Acids Res. 1980 Dec 11;8(23):5779–5794. doi: 10.1093/nar/8.23.5779. [DOI] [PMC free article] [PubMed] [Google Scholar]
  344. Ruiz-Vazquez R., Ruiz-Carillo A. Construction of chimeric plasmids containing histone H5 cDNA from hen erythrocyte. DNA sequence of a fragment derived from the 5' region of H5 mRNA. Nucleic Acids Res. 1982 Mar 25;10(6):2093–2108. doi: 10.1093/nar/10.6.2093. [DOI] [PMC free article] [PubMed] [Google Scholar]
  345. Russell D. W., Spremulli L. L. Mechanism of action of the wheat germ ribosome dissociation factor: interaction with the 60 S subunit. Arch Biochem Biophys. 1980 May;201(2):518–526. doi: 10.1016/0003-9861(80)90540-8. [DOI] [PubMed] [Google Scholar]
  346. Russell P. R., Hall B. D. Structure of the Schizosaccharomyces pombe cytochrome c gene. Mol Cell Biol. 1982 Feb;2(2):106–116. doi: 10.1128/mcb.2.2.106. [DOI] [PMC free article] [PubMed] [Google Scholar]
  347. Röhl R., Nierhaus K. H. Assembly map of the large subunit (50S) of Escherichia coli ribosomes. Proc Natl Acad Sci U S A. 1982 Feb;79(3):729–733. doi: 10.1073/pnas.79.3.729. [DOI] [PMC free article] [PubMed] [Google Scholar]
  348. Sabol S., Sillero M. A., Iwasaki K., Ochoa S. Purification and properties of initiation factor F3. Nature. 1970 Dec 26;228(5278):1269–1273. doi: 10.1038/2281269a0. [DOI] [PubMed] [Google Scholar]
  349. Sacerdot C., Fayat G., Dessen P., Springer M., Plumbridge J. A., Grunberg-Manago M., Blanquet S. Sequence of a 1.26-kb DNA fragment containing the structural gene for E.coli initiation factor IF3: presence of an AUU initiator codon. EMBO J. 1982;1(3):311–315. doi: 10.1002/j.1460-2075.1982.tb01166.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  350. Sagher D., Grosfeld H., Edelman M. Large subunit ribulosebisphosphate carboxylase messenger RNA from Euglena chloroplasts. Proc Natl Acad Sci U S A. 1976 Mar;73(3):722–726. doi: 10.1073/pnas.73.3.722. [DOI] [PMC free article] [PubMed] [Google Scholar]
  351. Saito H., Richardson C. C. Processing of mRNA by ribonuclease III regulates expression of gene 1.2 of bacteriophage T7. Cell. 1981 Dec;27(3 Pt 2):533–542. doi: 10.1016/0092-8674(81)90395-0. [DOI] [PubMed] [Google Scholar]
  352. Salim M., Maden B. E. Nucleotide sequence of Xenopus laevis 18S ribosomal RNA inferred from gene sequence. Nature. 1981 May 21;291(5812):205–208. doi: 10.1038/291205a0. [DOI] [PubMed] [Google Scholar]
  353. Samols D. R., Hagenbuchle O., Gage L. P. Homology of the 3' terminal sequences of the 18S rRNA of Bombyx mori and the 16S rRNA of Escherchia coli. Nucleic Acids Res. 1979 Nov 10;7(5):1109–1119. doi: 10.1093/nar/7.5.1109. [DOI] [PMC free article] [PubMed] [Google Scholar]
  354. Samuel C. E., Rabinowitz J. C. Initiation of protein synthesis by folate-sufficient and folate-deficient Streptococcus faecalis R. Biochemical and biophysical properties of methionine transfer ribonucleic acid. J Biol Chem. 1974 Feb 25;249(4):1198–1206. [PubMed] [Google Scholar]
  355. Sanger F., Coulson A. R., Friedmann T., Air G. M., Barrell B. G., Brown N. L., Fiddes J. C., Hutchison C. A., 3rd, Slocombe P. M., Smith M. The nucleotide sequence of bacteriophage phiX174. J Mol Biol. 1978 Oct 25;125(2):225–246. doi: 10.1016/0022-2836(78)90346-7. [DOI] [PubMed] [Google Scholar]
  356. Sargan D. R., Gregory S. P., Butterworth P. H. A possible novel interaction between the 3'-end of 18 S ribosomal RNA and the 5'-leader sequence of many eukaryotic messenger RNAs. FEBS Lett. 1982 Oct 18;147(2):133–136. doi: 10.1016/0014-5793(82)81026-0. [DOI] [PubMed] [Google Scholar]
  357. Sasavage N. L., Smith M., Gillam S., Woychik R. P., Rottman F. M. Variation in the polyadenylylation site of bovine prolactin mRNA. Proc Natl Acad Sci U S A. 1982 Jan;79(2):223–227. doi: 10.1073/pnas.79.2.223. [DOI] [PMC free article] [PubMed] [Google Scholar]
  358. Scherer G. F., Walkinshaw M. D., Arnott S., Morré D. J. The ribosome binding sites recognized by E. coli ribosomes have regions with signal character in both the leader and protein coding segments. Nucleic Acids Res. 1980 Sep 11;8(17):3895–3907. doi: 10.1093/nar/8.17.3895. [DOI] [PMC free article] [PubMed] [Google Scholar]
  359. Schimmel P. R., Söll D. Aminoacyl-tRNA synthetases: general features and recognition of transfer RNAs. Annu Rev Biochem. 1979;48:601–648. doi: 10.1146/annurev.bi.48.070179.003125. [DOI] [PubMed] [Google Scholar]
  360. Schmid H. P., Köhler K., Setyono B. Possible involvement of messenger RNA-associated proteins in protein synthesis. J Cell Biol. 1982 Jun;93(3):893–898. doi: 10.1083/jcb.93.3.893. [DOI] [PMC free article] [PubMed] [Google Scholar]
  361. Schmitt M., Kyriatsoulis A., Gassen H. G. The context theory as applied to the decoding of the initiator tRNA by Escherichia coli ribosomes. Eur J Biochem. 1982 Jul;125(2):389–394. doi: 10.1111/j.1432-1033.1982.tb06695.x. [DOI] [PubMed] [Google Scholar]
  362. Schmitt M., Manderschied U., Kyriatsoulis A., Brinckmann U., Gassen H. G. Tetranucleotides as effectors for the binding of initiator tRNA to Escherichia coli ribosomes. Eur J Biochem. 1980 Aug;109(1):291–299. doi: 10.1111/j.1432-1033.1980.tb04794.x. [DOI] [PubMed] [Google Scholar]
  363. Schnare M. N., Gray M. W. 3'-Terminal sequence of wheat mitochondrial 18S ribosomal RNA: further evidence of a eubacterial evolutionary origin. Nucleic Acids Res. 1982 Jul 10;10(13):3921–3932. doi: 10.1093/nar/10.13.3921. [DOI] [PMC free article] [PubMed] [Google Scholar]
  364. Schnare M. N., Gray M. W. Nucleotide sequence of an exceptionally long 5.8S ribosomal RNA from Crithidia fasciculata. Nucleic Acids Res. 1982 Mar 25;10(6):2085–2092. doi: 10.1093/nar/10.6.2085. [DOI] [PMC free article] [PubMed] [Google Scholar]
  365. Schroeder H. W., Jr, Liarakos C. D., Gupta R. C., Randerath K., O'Malley B. W. Ribosome binding site analysis of ovalbumin messenger ribonucleic acid. Biochemistry. 1979 Dec 25;18(26):5798–5808. doi: 10.1021/bi00593a009. [DOI] [PubMed] [Google Scholar]
  366. Schwartz J. H., Meyer R., Eisenstadt J. M., Brawerman G. Involvement of N-formylmethionine in initiation of protein synthesis in cell-free extracts of Euglena gracilis. J Mol Biol. 1967 May 14;25(3):571–574. doi: 10.1016/0022-2836(67)90210-0. [DOI] [PubMed] [Google Scholar]
  367. Schwartz M., Roa M., Débarbouillé M. Mutations that affect lamB gene expression at a posttranscriptional level. Proc Natl Acad Sci U S A. 1981 May;78(5):2937–2941. doi: 10.1073/pnas.78.5.2937. [DOI] [PMC free article] [PubMed] [Google Scholar]
  368. Schümperli D., Howard B. H., Rosenberg M. Efficient expression of Escherichia coli galactokinase gene in mammalian cells. Proc Natl Acad Sci U S A. 1982 Jan;79(2):257–261. doi: 10.1073/pnas.79.2.257. [DOI] [PMC free article] [PubMed] [Google Scholar]
  369. Schümperli D., McKenney K., Sobieski D. A., Rosenberg M. Translational coupling at an intercistronic boundary of the Escherichia coli galactose operon. Cell. 1982 Oct;30(3):865–871. doi: 10.1016/0092-8674(82)90291-4. [DOI] [PubMed] [Google Scholar]
  370. Selker E., Yanofsky C. Nucleotide sequence of the trpC-trpB intercistronic region from Salmonella typhimurium. J Mol Biol. 1979 May 15;130(2):135–143. doi: 10.1016/0022-2836(79)90422-4. [DOI] [PubMed] [Google Scholar]
  371. Setyono B., Greenberg J. R. Proteins associated with poly(A) and other regions of mRNA and hnRNA molecules as investigated by crosslinking. Cell. 1981 Jun;24(3):775–783. doi: 10.1016/0092-8674(81)90103-3. [DOI] [PubMed] [Google Scholar]
  372. Setzer D. R., McGrogan M., Nunberg J. H., Schimke R. T. Size heterogeneity in the 3' end of dihydrofolate reductase messenger RNAs in mouse cells. Cell. 1980 Nov;22(2 Pt 2):361–370. doi: 10.1016/0092-8674(80)90346-3. [DOI] [PubMed] [Google Scholar]
  373. Setzer D. R., McGrogan M., Schimke R. T. Nucleotide sequence surrounding multiple polyadenylation sites in the mouse dihydrofolate reductase gene. J Biol Chem. 1982 May 10;257(9):5143–5147. [PubMed] [Google Scholar]
  374. Shafritz D. A., Weinstein J. A., Safer B., Merrick W. C., Weber L. A., Hickey E. D., Baglioni C. Evidence for role of m7G5'-phosphate group in recognition of eukaryotic mRNA by initiation factor IF-M3. Nature. 1976 May 27;261(5558):291–294. doi: 10.1038/261291a0. [DOI] [PubMed] [Google Scholar]
  375. Shani M., Nudel U., Zevin-Sonkin D., Zakut R., Givol D., Katcoff D., Carmon Y., Reiter J., Frischauf A. M., Yaffe D. Skeletal muscle actin mRNA. Characterization of the 3' untranslated region. Nucleic Acids Res. 1981 Feb 11;9(3):579–589. doi: 10.1093/nar/9.3.579. [DOI] [PMC free article] [PubMed] [Google Scholar]
  376. Sharp P. A. Speculations on RNA splicing. Cell. 1981 Mar;23(3):643–646. doi: 10.1016/0092-8674(81)90425-6. [DOI] [PubMed] [Google Scholar]
  377. Shatkin A. J. Capping of eucaryotic mRNAs. Cell. 1976 Dec;9(4 Pt 2):645–653. doi: 10.1016/0092-8674(76)90128-8. [DOI] [PubMed] [Google Scholar]
  378. Shatsky I. N., Mochalova L. V., Kojouharova M. S., Bogdanov A. A., Vasiliev V. D. Localization of the 3' end of Escherichia coli 16 S RNA by electron microscopy of antibody-labelled subunits. J Mol Biol. 1979 Oct 9;133(4):501–515. doi: 10.1016/0022-2836(79)90404-2. [DOI] [PubMed] [Google Scholar]
  379. Shen L. P., Pictet R. L., Rutter W. J. Human somatostatin I: sequence of the cDNA. Proc Natl Acad Sci U S A. 1982 Aug;79(15):4575–4579. doi: 10.1073/pnas.79.15.4575. [DOI] [PMC free article] [PubMed] [Google Scholar]
  380. Shenk T. Transcriptional control regions: nucleotide sequence requirements for initiation by RNA polymerase II and III. Curr Top Microbiol Immunol. 1981;93:25–46. doi: 10.1007/978-3-642-68123-3_3. [DOI] [PubMed] [Google Scholar]
  381. Shepard H. M., Yelverton E., Goeddel D. V. Increased synthesis in E. coli of fibroblast and leukocyte interferons through alterations in ribosome binding sites. DNA. 1982;1(2):125–131. doi: 10.1089/dna.1.1982.1.125. [DOI] [PubMed] [Google Scholar]
  382. Sherman F., McKnight G., Stewart J. W. AUG is the only initiation codon in eukaryotes. Biochim Biophys Acta. 1980 Sep 19;609(2):343–346. doi: 10.1016/0005-2787(80)90246-4. [DOI] [PubMed] [Google Scholar]
  383. Sherman F., Stewart J. W., Schweingruber A. M. Mutants of yeast initiating translation of iso-1-cytochrome c within a region spanning 37 nucleotides. Cell. 1980 May;20(1):215–222. doi: 10.1016/0092-8674(80)90249-4. [DOI] [PubMed] [Google Scholar]
  384. Sherwood L. M., Burstein Y., Schechter I. Primary structure of the NH2-terminal extra piece of the precursor to human placental lactogen. Proc Natl Acad Sci U S A. 1979 Aug;76(8):3819–3823. doi: 10.1073/pnas.76.8.3819. [DOI] [PMC free article] [PubMed] [Google Scholar]
  385. Shih D. S., Kaesberg P. Translation of brome mosaic viral ribonucleic acid in a cell-free system derived from wheat embryo. Proc Natl Acad Sci U S A. 1973 Jun;70(6):1799–1803. doi: 10.1073/pnas.70.6.1799. [DOI] [PMC free article] [PubMed] [Google Scholar]
  386. Shine J., Dalgarno L. Occurrence of heat-dissociable ribosomal RNA in insects: the presence of three polynucleotide chains in 26 S RNA from cultured Aedes aegypti cells. J Mol Biol. 1973 Mar 25;75(1):57–72. doi: 10.1016/0022-2836(73)90528-7. [DOI] [PubMed] [Google Scholar]
  387. Shine J., Dalgarno L. The 3'-terminal sequence of Escherichia coli 16S ribosomal RNA: complementarity to nonsense triplets and ribosome binding sites. Proc Natl Acad Sci U S A. 1974 Apr;71(4):1342–1346. doi: 10.1073/pnas.71.4.1342. [DOI] [PMC free article] [PubMed] [Google Scholar]
  388. Siekierka J., Mauser L., Ochoa S. Mechanism of polypeptide chain initiation in eukaryotes and its control by phosphorylation of the alpha subunit of initiation factor 2. Proc Natl Acad Sci U S A. 1982 Apr;79(8):2537–2540. doi: 10.1073/pnas.79.8.2537. [DOI] [PMC free article] [PubMed] [Google Scholar]
  389. Singer B. S., Gold L., Shinedling S. T., Colkitt M., Hunter L. R., Pribnow D., Nelson M. A. Analysis in vivo of translational mutants of the rIIB cistron of bacteriophage T4. J Mol Biol. 1981 Jul 5;149(3):405–432. doi: 10.1016/0022-2836(81)90479-4. [DOI] [PubMed] [Google Scholar]
  390. Smiley B. L., Lupski J. R., Svec P. S., McMacken R., Godson G. N. Sequences of the Escherichia coli dnaG primase gene and regulation of its expression. Proc Natl Acad Sci U S A. 1982 Aug;79(15):4550–4554. doi: 10.1073/pnas.79.15.4550. [DOI] [PMC free article] [PubMed] [Google Scholar]
  391. Smith A. E., Kamen R., Mangel W. F., Shure H., Wheeler T. Location of the sequences coding for capsid proteins VP1 and VP2 on polyoma virus DNA. Cell. 1976 Nov;9(3):481–487. doi: 10.1016/0092-8674(76)90093-3. [DOI] [PubMed] [Google Scholar]
  392. Smith A. E., Marcker K. A. Cytoplasmic methionine transfer RNAs from eukaryotes. Nature. 1970 May 16;226(5246):607–610. doi: 10.1038/226607a0. [DOI] [PubMed] [Google Scholar]
  393. Smith A. E., Marcker K. A. N-formylmethionyl transfer RNA in mitochondria from yeast and rat liver. J Mol Biol. 1968 Dec 14;38(2):241–243. doi: 10.1016/0022-2836(68)90409-9. [DOI] [PubMed] [Google Scholar]
  394. Smith R. E., Clark J. M., Jr Effect of capping upon the mRNA properties of satellite tobacco necrosis virus ribonucleic acid. Biochemistry. 1979 Apr 3;18(7):1366–1371. doi: 10.1021/bi00574a037. [DOI] [PubMed] [Google Scholar]
  395. Snyder M., Hunkapiller M., Yuen D., Silvert D., Fristrom J., Davidson N. Cuticle protein genes of Drosophila: structure, organization and evolution of four clustered genes. Cell. 1982 Jul;29(3):1027–1040. doi: 10.1016/0092-8674(82)90466-4. [DOI] [PubMed] [Google Scholar]
  396. Sonenberg N., Guertin D., Cleveland D., Trachsel H. Probing the function of the eucaryotic 5' cap structure by using a monoclonal antibody directed against cap-binding proteins. Cell. 1981 Dec;27(3 Pt 2):563–572. doi: 10.1016/0092-8674(81)90398-6. [DOI] [PubMed] [Google Scholar]
  397. Sonenberg N., Morgan M. A., Merrick W. C., Shatkin A. J. A polypeptide in eukaryotic initiation factors that crosslinks specifically to the 5'-terminal cap in mRNA. Proc Natl Acad Sci U S A. 1978 Oct;75(10):4843–4847. doi: 10.1073/pnas.75.10.4843. [DOI] [PMC free article] [PubMed] [Google Scholar]
  398. Soreq H., Sagar A. D., Sehgal P. B. Translational activity and functional stability of human fibroblast beta 1 and beta 2 interferon mRNAs lacking 3'-terminal RNA sequences. Proc Natl Acad Sci U S A. 1981 Mar;78(3):1741–1745. doi: 10.1073/pnas.78.3.1741. [DOI] [PMC free article] [PubMed] [Google Scholar]
  399. Southern P. J., Howard B. H., Berg P. Construction and characterization of SV40 recombinants with beta-globin cDNA substitutions in their early regions. J Mol Appl Genet. 1981;1(3):177–190. [PubMed] [Google Scholar]
  400. Spencer D. F., Bonen L., Gray M. W. Primary sequence of wheat mitochondrial 5S ribosomal ribonucleic acid: functional and evolutionary implications. Biochemistry. 1981 Jul 7;20(14):4022–4029. doi: 10.1021/bi00517a011. [DOI] [PubMed] [Google Scholar]
  401. Sprague K. U., Steitz J. A., Grenley R. M., Stocking C. E. 3' terminal sequences of 16S rRNA do not explain translational specificity differences between E. coli and B. stearothermophilus ribosomes. Nature. 1977 Jun 2;267(5610):462–465. doi: 10.1038/267462a0. [DOI] [PubMed] [Google Scholar]
  402. Spremulli L. L. Chloroplast elongation factor Tu: evidence that it is the product of a chloroplast gene in Euglena. Arch Biochem Biophys. 1982 Apr 1;214(2):734–741. doi: 10.1016/0003-9861(82)90080-7. [DOI] [PubMed] [Google Scholar]
  403. Steege D. A. 5'-Terminal nucleotide sequence of Escherichia coli lactose repressor mRNA: features of translational initiation and reinitiation sites. Proc Natl Acad Sci U S A. 1977 Oct;74(10):4163–4167. doi: 10.1073/pnas.74.10.4163. [DOI] [PMC free article] [PubMed] [Google Scholar]
  404. Steege D. A., Graves M. C., Spremulli L. L. Euglena gracilis chloroplast small subunit rRNA. Sequence and base pairing potential of the 3' terminus, cleavage by colicin E3. J Biol Chem. 1982 Sep 10;257(17):10430–10439. [PubMed] [Google Scholar]
  405. Steitz J. A., Jakes K. How ribosomes select initiator regions in mRNA: base pair formation between the 3' terminus of 16S rRNA and the mRNA during initiation of protein synthesis in Escherichia coli. Proc Natl Acad Sci U S A. 1975 Dec;72(12):4734–4738. doi: 10.1073/pnas.72.12.4734. [DOI] [PMC free article] [PubMed] [Google Scholar]
  406. Steitz J. A. Oligonucleotide sequence of replicase initiation site in Q RNA. Nat New Biol. 1972 Mar 22;236(64):71–75. doi: 10.1038/newbio236071a0. [DOI] [PubMed] [Google Scholar]
  407. Steitz J. A. Polypeptide chain initiation: nucleotide sequences of the three ribosomal binding sites in bacteriophage R17 RNA. Nature. 1969 Dec 6;224(5223):957–964. doi: 10.1038/224957a0. [DOI] [PubMed] [Google Scholar]
  408. Steitz J. A. Specific recognition of non-initiator regions in RNA bacteriophage messengers by ribosomes of Bacillus stearothermophilus. J Mol Biol. 1973 Jan;73(1):1–16. doi: 10.1016/0022-2836(73)90155-1. [DOI] [PubMed] [Google Scholar]
  409. Steitz J. A., Steege D. A. Characterization of two mRNA-rRNA complexes implicated in the initiation of protein biosynthesis. J Mol Biol. 1977 Aug 25;114(4):545–558. doi: 10.1016/0022-2836(77)90177-2. [DOI] [PubMed] [Google Scholar]
  410. Steitz J. A., Wahba A. J., Laughrea M., Moore P. B. Differential requirements for polypeptide chain initiation complex formation at the three bacteriophage R17 initiator regions. Nucleic Acids Res. 1977 Jan;4(1):1–15. doi: 10.1093/nar/4.1.1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  411. Stewart J. W., Sherman F., Shipman N. A., Jackson M. Identification and mutational relocation of the AUG codon initiating translation of iso-1-cytochrome c in yeast. J Biol Chem. 1971 Dec 25;246(24):7429–7445. [PubMed] [Google Scholar]
  412. Stiegler G. L., Matthews H. M., Bingham S. E., Hallick R. B. The gene for the large subunit of ribulose-1,5-bisphosphate carboxylase in Euglena gracilis chloroplast DNA: location, polarity, cloning, and evidence for an intervening sequence. Nucleic Acids Res. 1982 Jun 11;10(11):3427–3444. doi: 10.1093/nar/10.11.3427. [DOI] [PMC free article] [PubMed] [Google Scholar]
  413. Stiegler P., Carbon P., Ebel J. P., Ehresmann C. A general secondary-structure model for procaryotic and eucaryotic RNAs from the small ribosomal subunits. Eur J Biochem. 1981 Dec;120(3):487–495. doi: 10.1111/j.1432-1033.1981.tb05727.x. [DOI] [PubMed] [Google Scholar]
  414. Stiles J. I., Szostak J. W., Young A. T., Wu R., Consaul S., Sherman F. DNA sequence of a mutation in the leader region of the yeast iso-1-cytochrome c mRNA. Cell. 1981 Jul;25(1):277–284. doi: 10.1016/0092-8674(81)90253-1. [DOI] [PubMed] [Google Scholar]
  415. Stormo G. D., Schneider T. D., Gold L. M. Characterization of translational initiation sites in E. coli. Nucleic Acids Res. 1982 May 11;10(9):2971–2996. doi: 10.1093/nar/10.9.2971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  416. Stringer E. A., Sarkar P., Maitra U. Function of initiation factor 1 in the binding and release of initiation factor 2 from ribosomal initiation complexes in Escherichia coli. J Biol Chem. 1977 Mar 10;252(5):1739–1744. [PubMed] [Google Scholar]
  417. Stroynowski I., van Cleemput M., Yanofsky C. Superattenuation in the tryptophan operon of Serratia marcescens. Nature. 1982 Jul 1;298(5869):38–41. doi: 10.1038/298038a0. [DOI] [PubMed] [Google Scholar]
  418. Struhl K., Davis R. W. Promotor mutants of the yeast his3 gene. J Mol Biol. 1981 Nov 5;152(3):553–568. doi: 10.1016/0022-2836(81)90268-0. [DOI] [PubMed] [Google Scholar]
  419. Struhl K., Stinchcomb D. T., Davis R. W. A physiological study of functional expression in Escherichia coli of the cloned yeast imidazoleglycerolphosphate dehydratase gene. J Mol Biol. 1980 Jan 25;136(3):291–307. doi: 10.1016/0022-2836(80)90375-7. [DOI] [PubMed] [Google Scholar]
  420. Stubbs J. D., Kaesberg P. Amino acid incorporation in an Escherichia coli cell-free system directed by bromegrass mosaic virus ribonucleic acid. Virology. 1967 Nov;33(3):385–397. doi: 10.1016/0042-6822(67)90114-6. [DOI] [PubMed] [Google Scholar]
  421. Stöffler-Meilicke M., Stöffler G., Odom O. W., Zinn A., Kramer G., Hardesty B. Localization of 3' ends of 5S and 23S rRNAs in reconstituted subunits of Escherichia coli ribosomes. Proc Natl Acad Sci U S A. 1981 Sep;78(9):5538–5542. doi: 10.1073/pnas.78.9.5538. [DOI] [PMC free article] [PubMed] [Google Scholar]
  422. Subramanian A. R., Davis B. D. Activity of initiation factor F3 in dissociating Escherichia coli ribosomes. Nature. 1970 Dec 26;228(5278):1273–1275. doi: 10.1038/2281273a0. [DOI] [PubMed] [Google Scholar]
  423. Sundari R. M., Pelka H., Schulman L. H. Structural requirements of Escherichia coli formylmethionyl transfer ribonucleic acid for ribosome binding and initiation of protein synthesis. J Biol Chem. 1977 Jun 10;252(11):3941–3944. [PubMed] [Google Scholar]
  424. Sundari R. M., Stringer E. A., Schulman L. H., Maitra U. Interaction of bacterial initiation factor 2 with initiator tRNA. J Biol Chem. 1976 Jun 10;251(11):3338–3345. [PubMed] [Google Scholar]
  425. Sures I., Levy S., Kedes L. H. Leader sequences of Strongylocentrotus purpuratus histone mRNAs start at a unique heptanucleotide common to all five histone genes. Proc Natl Acad Sci U S A. 1980 Mar;77(3):1265–1269. doi: 10.1073/pnas.77.3.1265. [DOI] [PMC free article] [PubMed] [Google Scholar]
  426. Swanstrom R., Varmus H. E., Bishop J. M. Nucleotide sequence of the 5' noncoding region and part of the gag gene of Rous sarcoma virus. J Virol. 1982 Feb;41(2):535–541. doi: 10.1128/jvi.41.2.535-541.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  427. Sánchez-Madrid F., Vidales F. J., Ballesta J. P. Functional role of acidic ribosomal proteins. Interchangeability of proteins from bacterial and eukaryotic cells. Biochemistry. 1981 May 26;20(11):3263–3266. doi: 10.1021/bi00514a043. [DOI] [PubMed] [Google Scholar]
  428. Takaiwa F., Sugiura M. The complete nucleotide sequence of a 23-S rRNA gene from tobacco chloroplasts. Eur J Biochem. 1982 May;124(1):13–19. doi: 10.1111/j.1432-1033.1982.tb05901.x. [DOI] [PubMed] [Google Scholar]
  429. Takeishi K., Ukita T., Nishimura S. Characterization of two species of methionine transfer ribonucleic acid from bakers' yeast. J Biol Chem. 1968 Nov 10;243(21):5761–5768. [PubMed] [Google Scholar]
  430. Talkington C. A., Leder P. Rescuing the in vitro function of a globin pseudogene promoter. Nature. 1982 Jul 8;298(5870):192–195. doi: 10.1038/298192a0. [DOI] [PubMed] [Google Scholar]
  431. Tanaka T., Wool I. G., Stöffler G. The effect of antibodies against Escherichia coli small ribosomal subunit proteins on protein synthesis by rat liver ribosomes. J Biol Chem. 1980 May 10;255(9):3832–3834. [PubMed] [Google Scholar]
  432. Taniguchi T., Weissmann C. Escherichia coli ribosomes bind to non-initiator sites of Q beta RNA in the absence of formylmethionyl-tRNA. J Mol Biol. 1979 Mar 15;128(4):481–500. doi: 10.1016/0022-2836(79)90289-4. [DOI] [PubMed] [Google Scholar]
  433. Taniguchi T., Weissmann C. Inhibition of Qbeta RNA 70S ribosome initiation complex formation by an oligonucleotide complementary to the 3' terminal region of E. coli 16S ribosomal RNA. Nature. 1978 Oct 26;275(5682):770–772. doi: 10.1038/275770a0. [DOI] [PubMed] [Google Scholar]
  434. Thach R. E., Sundararajan T. A., Dewey K. F., Brown J. C., Doty P. Translation of synthetic messenger RNA. Cold Spring Harb Symp Quant Biol. 1966;31:85–97. doi: 10.1101/sqb.1966.031.01.015. [DOI] [PubMed] [Google Scholar]
  435. Thomas A., Spaan W., van Steeg H., Voorma H. O., Benne R. Mode of action of protein synthesis initiation factor eIF-1 from rabbit reticulocytes. FEBS Lett. 1980 Jul 11;116(1):67–71. doi: 10.1016/0014-5793(80)80530-8. [DOI] [PubMed] [Google Scholar]
  436. Thompson H. A., Sadnik I., Scheinbuks J., Moldave K. Studies on native ribosomal subunits from rat liver. Purification and characterization of a ribosome dissociation factor. Biochemistry. 1977 May 17;16(10):2221–2230. doi: 10.1021/bi00629a028. [DOI] [PubMed] [Google Scholar]
  437. Thummel C. S., Burgess T. L., Tjian R. Properties of simian virus 40 small t antigen overproduced in bacteria. J Virol. 1981 Feb;37(2):683–697. doi: 10.1128/jvi.37.2.683-697.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  438. Tohdoh N., Sugiura M. The complete nucleotide sequence of 16S ribosomal RNA gene from tobacco chloroplasts. Gene. 1982 Feb;17(2):213–218. doi: 10.1016/0378-1119(82)90074-9. [DOI] [PubMed] [Google Scholar]
  439. Trachsel H., Erni B., Schreier M. H., Staehelin T. Initiation of mammalian protein synthesis. II. The assembly of the initiation complex with purified initiation factors. J Mol Biol. 1977 Nov;116(4):755–767. doi: 10.1016/0022-2836(77)90269-8. [DOI] [PubMed] [Google Scholar]
  440. Treisman R. Characterisation of polyoma late mRNA leader sequences by molecular cloning and DNA sequence analysis. Nucleic Acids Res. 1980 Nov 11;8(21):4867–4888. doi: 10.1093/nar/8.21.4867. [DOI] [PMC free article] [PubMed] [Google Scholar]
  441. Trempe M. R., Glitz D. G. Chloroplast ribosome structure. Electron microscopy of ribosomal subunits and localization of N6,N6-dimethyladenosine by immunoelectronmicroscopy. J Biol Chem. 1981 Nov 25;256(22):11873–11879. [PubMed] [Google Scholar]
  442. Tuite M. F., Plesset J., Moldave K., McLaughlin C. S. Faithful and efficient translation of homologous and heterologous mRNAs in an mRNA-dependent cell-free system from Saccharomyces cerevisiae. J Biol Chem. 1980 Sep 25;255(18):8761–8766. [PubMed] [Google Scholar]
  443. Ulbrich B., Czempiel W., Bass R. Mammalian mitochondrial ribosomes. Studies on the exchangeability of polypeptide chain elongation factors from bacterial and mitochondrial systems. Eur J Biochem. 1980 Jul;108(2):337–343. doi: 10.1111/j.1432-1033.1980.tb04728.x. [DOI] [PubMed] [Google Scholar]
  444. Valenzuela D. M., Chaudhuri A., Maitra U. Eukaryotic ribosomal subunit anti-association activity of calf liver is contained in a single polypeptide chain protein of Mr = 25,500 (eukaryotic initiation factor 6). J Biol Chem. 1982 Jul 10;257(13):7712–7719. [PubMed] [Google Scholar]
  445. Valenzuela P., Medina A., Rutter W. J., Ammerer G., Hall B. D. Synthesis and assembly of hepatitis B virus surface antigen particles in yeast. Nature. 1982 Jul 22;298(5872):347–350. doi: 10.1038/298347a0. [DOI] [PubMed] [Google Scholar]
  446. Van Duin J., Overbeek G. P., Backendorf C. Functional recognition of phage RNA by 30-S ribosomal subunits in the absence of initiator tRNA. Eur J Biochem. 1980 Sep;110(2):593–597. doi: 10.1111/j.1432-1033.1980.tb04903.x. [DOI] [PubMed] [Google Scholar]
  447. Veldman G. M., Klootwijk J., de Regt V. C., Planta R. J., Branlant C., Krol A., Ebel J. P. The primary and secondary structure of yeast 26S rRNA. Nucleic Acids Res. 1981 Dec 21;9(24):6935–6952. doi: 10.1093/nar/9.24.6935. [DOI] [PMC free article] [PubMed] [Google Scholar]
  448. Vermeer C., van Alphen W., van Knippenberg P., Bosch L. Initiation factor-dependent binding of MS2 RNA to 30-S ribosomes and the recycling of IF-3. Eur J Biochem. 1973 Dec 3;40(1):295–308. doi: 10.1111/j.1432-1033.1973.tb03197.x. [DOI] [PubMed] [Google Scholar]
  449. Walker R. T., RajBhandary U. L. The nucleotide sequence of formylmethionine tRNA from Mycoplasma mycoides sp. capri. Nucleic Acids Res. 1978 Jan;5(1):57–70. doi: 10.1093/nar/5.1.57. [DOI] [PMC free article] [PubMed] [Google Scholar]
  450. Walker W. F. Proposed sequence homology between the 5'-end regions of prokaryotic 23 S rRNA and eukaryotic 28 S rRNA. Relevance to the hypothesis that 5.8 S rRNA is homologous to the 5'-end region of 23 S rRNA. FEBS Lett. 1981 Apr 20;126(2):150–151. doi: 10.1016/0014-5793(81)80228-1. [DOI] [PubMed] [Google Scholar]
  451. Wallis J. W., Hereford L., Grunstein M. Histone H2B genes of yeast encode two different proteins. Cell. 1980 Dec;22(3):799–805. doi: 10.1016/0092-8674(80)90556-5. [DOI] [PubMed] [Google Scholar]
  452. Walter P., Blobel G. Translocation of proteins across the endoplasmic reticulum III. Signal recognition protein (SRP) causes signal sequence-dependent and site-specific arrest of chain elongation that is released by microsomal membranes. J Cell Biol. 1981 Nov;91(2 Pt 1):557–561. doi: 10.1083/jcb.91.2.557. [DOI] [PMC free article] [PubMed] [Google Scholar]
  453. Warner J. R., Gorenstein C. The synthesis of eucaryotic ribosomal proteins in vitro. Cell. 1977 May;11(1):201–212. doi: 10.1016/0092-8674(77)90331-2. [DOI] [PubMed] [Google Scholar]
  454. Watson J. C., Surzycki S. J. Extensive sequence homology in the DNA coding for elongation factor Tu from Escherichia coli and the Chlamydomonas reinhardtii chloroplast. Proc Natl Acad Sci U S A. 1982 Apr;79(7):2264–2267. doi: 10.1073/pnas.79.7.2264. [DOI] [PMC free article] [PubMed] [Google Scholar]
  455. Watson R. J., Vande Woude G. F. DNA sequence of an immediate-early gene (IEmRNA-5) of herpes simplex virus type I. Nucleic Acids Res. 1982 Feb 11;10(3):979–991. doi: 10.1093/nar/10.3.979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  456. Weber H., Billeter M. A., Kahane S., Weissmann C., Hindley J., Porter A. Molecular basis for repressor activity of Q replicase. Nat New Biol. 1972 Jun 7;237(75):166–170. doi: 10.1038/newbio237166a0. [DOI] [PubMed] [Google Scholar]
  457. Weber L. A., Hickey E. D., Baglioni C. Influence of potassium salt concentration and temperature on inhibition of mRNA translation by 7-methylguanosine5'-monophosphate. J Biol Chem. 1978 Jan 10;253(1):178–183. [PubMed] [Google Scholar]
  458. Weiss S. R., Varmus H. E., Bishop J. M. The size and genetic composition of virus-specific RNAs in the cytoplasm of cells producing avian sarcoma-leukosis viruses. Cell. 1977 Dec;12(4):983–992. doi: 10.1016/0092-8674(77)90163-5. [DOI] [PubMed] [Google Scholar]
  459. Wengler G., Wengler G., Gross H. S. Replicative form of Semliki Forest virus RNA contains an unpaired guanosine. Nature. 1979 Dec 13;282(5740):754–756. doi: 10.1038/282754a0. [DOI] [PubMed] [Google Scholar]
  460. White B. N., Bayley S. T. Methionine transfer RNAs from the extreme halophile, Halobacterium cutirubrum. Biochim Biophys Acta. 1972 Jul 31;272(4):583–587. doi: 10.1016/0005-2787(72)90513-8. [DOI] [PubMed] [Google Scholar]
  461. Wieringa B., van der Zwaag-Gerritsen J., Mulder J., Ab G., Gruber M. Translation in vivo and in vitro of mRNAs coding for vitellogenin, serum albumin and very-low-density lipoprotein II from chicken liver. A difference in translational efficiency. Eur J Biochem. 1981 Mar;114(3):635–641. doi: 10.1111/j.1432-1033.1981.tb05191.x. [DOI] [PubMed] [Google Scholar]
  462. Wild M. A., Gall J. G. An intervening sequence in the gene coding for 25S ribosomal RNA of Tetrahymena pigmentosa. Cell. 1979 Mar;16(3):565–573. doi: 10.1016/0092-8674(79)90030-8. [DOI] [PubMed] [Google Scholar]
  463. Wittmann H. G. Components of bacterial ribosomes. Annu Rev Biochem. 1982;51:155–183. doi: 10.1146/annurev.bi.51.070182.001103. [DOI] [PubMed] [Google Scholar]
  464. Wold F. In vivo chemical modification of proteins (post-translational modification). Annu Rev Biochem. 1981;50:783–814. doi: 10.1146/annurev.bi.50.070181.004031. [DOI] [PubMed] [Google Scholar]
  465. Woo N. H., Roe B. A., Rich A. Three-dimensional structure of Escherichia coli initiator tRNAfMet. Nature. 1980 Jul 24;286(5771):346–351. doi: 10.1038/286346a0. [DOI] [PubMed] [Google Scholar]
  466. Wool I. G. The structure and function of eukaryotic ribosomes. Annu Rev Biochem. 1979;48:719–754. doi: 10.1146/annurev.bi.48.070179.003443. [DOI] [PubMed] [Google Scholar]
  467. Woolford J. L., Jr, Rosbash M. Ribosomal protein genes rp 39(10 - 78), rp 39(11 - 40), rp 51, and rp 52 are not contiguous to other ribosomal protein genes in the Saccharomyces cerevisiae genome. Nucleic Acids Res. 1981 Oct 10;9(19):5021–5036. doi: 10.1093/nar/9.19.5021. [DOI] [PMC free article] [PubMed] [Google Scholar]
  468. Wrede P., Woo N. H., Rich A. Initiator tRNAs have a unique anticodon loop conformation. Proc Natl Acad Sci U S A. 1979 Jul;76(7):3289–3293. doi: 10.1073/pnas.76.7.3289. [DOI] [PMC free article] [PubMed] [Google Scholar]
  469. Yamaguchi K., Hidaka S., Miura K. Relationship between structure of the 5' noncoding region of viral mRNA and efficiency in the initiation step of protein synthesis in a eukaryotic system. Proc Natl Acad Sci U S A. 1982 Feb;79(4):1012–1016. doi: 10.1073/pnas.79.4.1012. [DOI] [PMC free article] [PubMed] [Google Scholar]
  470. Yanofsky C. Attenuation in the control of expression of bacterial operons. Nature. 1981 Feb 26;289(5800):751–758. doi: 10.1038/289751a0. [DOI] [PubMed] [Google Scholar]
  471. Yanofsky C., Platt T., Crawford I. P., Nichols B. P., Christie G. E., Horowitz H., VanCleemput M., Wu A. M. The complete nucleotide sequence of the tryptophan operon of Escherichia coli. Nucleic Acids Res. 1981 Dec 21;9(24):6647–6668. doi: 10.1093/nar/9.24.6647. [DOI] [PMC free article] [PubMed] [Google Scholar]
  472. Yates J. L., Dean D., Strycharz W. A., Nomura M. E. coli ribosomal protein L10 inhibits translation of L10 and L7/L12 mRNAs by acting at a single site. Nature. 1981 Nov 12;294(5837):190–192. doi: 10.1038/294190a0. [DOI] [PubMed] [Google Scholar]
  473. Yen T. S., Webster R. E. Translational control of bacteriophage f1 gene II and gene X proteins by gene V protein. Cell. 1982 Jun;29(2):337–345. doi: 10.1016/0092-8674(82)90150-7. [DOI] [PubMed] [Google Scholar]
  474. Yokota T., Sugisaki H., Takanami M., Kaziro Y. The nucleotide sequence of the cloned tufA gene of Escherichia coli. Gene. 1980 Dec;12(1-2):25–31. doi: 10.1016/0378-1119(80)90012-8. [DOI] [PubMed] [Google Scholar]
  475. Yoo O. J., Powell C. T., Agarwal K. L. Molecular cloning and nucleotide sequence of full-length of cDNA coding for porcine gastrin. Proc Natl Acad Sci U S A. 1982 Feb;79(4):1049–1053. doi: 10.1073/pnas.79.4.1049. [DOI] [PMC free article] [PubMed] [Google Scholar]
  476. Young I. G., Rogers B. L., Campbell H. D., Jaworowski A., Shaw D. C. Nucleotide sequence coding for the respiratory NADH dehydrogenase of Escherichia coli. UUG initiation codon. Eur J Biochem. 1981 May;116(1):165–170. doi: 10.1111/j.1432-1033.1981.tb05314.x. [DOI] [PubMed] [Google Scholar]
  477. Young R. A., Hagenbüchle O., Schibler U. A single mouse alpha-amylase gene specifies two different tissue-specific mRNAs. Cell. 1981 Feb;23(2):451–458. doi: 10.1016/0092-8674(81)90140-9. [DOI] [PubMed] [Google Scholar]
  478. Yuan R. C., Steitz J. A., Moore P. B., Crothers D. M. The 3' terminus of 16S rRNA: secondary structure and interaction with ribosomal protein S1. Nucleic Acids Res. 1979 Dec 20;7(8):2399–2418. doi: 10.1093/nar/7.8.2399. [DOI] [PMC free article] [PubMed] [Google Scholar]
  479. Yuckenberg P. D., Phillips S. L. Oligoadenylate is present in the mitochondrial RNA of Saccharomyces cerevisiae. Mol Cell Biol. 1982 Apr;2(4):450–456. doi: 10.1128/mcb.2.4.450. [DOI] [PMC free article] [PubMed] [Google Scholar]
  480. Zagórska L., Chroboczek J., Klita S., Szafrański P. Effect of secondary structure of messenger ribonucleic acid on the formation of initiation complexes with prokaryotic and eukaryotic ribosomes. Eur J Biochem. 1982 Feb;122(2):265–269. doi: 10.1111/j.1432-1033.1982.tb05876.x. [DOI] [PubMed] [Google Scholar]
  481. Zain S., Sambrook J., Roberts R. J., Keller W., Fried M., Dunn A. R. Nucleotide sequence analysis of the leader segments in a cloned copy of adenovirus 2 fiber mRNA. Cell. 1979 Apr;16(4):851–861. doi: 10.1016/0092-8674(79)90100-4. [DOI] [PubMed] [Google Scholar]
  482. Zalkin H., Yanofsky C., Squires C. L. Regulated in vitro synthesis of Escherichia coli tryptophan operon messenger ribonucleic acid and enzymes. J Biol Chem. 1974 Jan 25;249(2):465–475. [PubMed] [Google Scholar]
  483. Zalkin H., Yanofsky C. Yeast gene TRP5: structure, function, regulation. J Biol Chem. 1982 Feb 10;257(3):1491–1500. [PubMed] [Google Scholar]
  484. Zeevi M., Nevins J. R., Darnell J. E., Jr Newly formed mRNA lacking polyadenylic acid enters the cytoplasm and the polyribosomes but has a shorter half-life in the absence of polyadenylic acid. Mol Cell Biol. 1982 May;2(5):517–525. doi: 10.1128/mcb.2.5.517. [DOI] [PMC free article] [PubMed] [Google Scholar]
  485. Ziff E. B., Evans R. M. Coincidence of the promoter and capped 5' terminus of RNA from the adenovirus 2 major late transcription unit. Cell. 1978 Dec;15(4):1463–1475. doi: 10.1016/0092-8674(78)90070-3. [DOI] [PubMed] [Google Scholar]
  486. Zipori P., Bosch L., van Duin J. Translation of MS2 RNA in vitro in the absence of initiation factor IF-3. Eur J Biochem. 1978 Dec 1;92(1):235–241. doi: 10.1111/j.1432-1033.1978.tb12741.x. [DOI] [PubMed] [Google Scholar]
  487. Zurawski G., Perrot B., Bottomley W., Whitfeld P. R. The structure of the gene for the large subunit of ribulose 1,5-bisphosphate carboxylase from spinach chloroplast DNA. Nucleic Acids Res. 1981 Jul 24;9(14):3251–3270. doi: 10.1093/nar/9.14.3251. [DOI] [PMC free article] [PubMed] [Google Scholar]
  488. van Duin J., Kurland C. G., Dondon J., Grunberg-Manago M. Near neighbors of IF3 bound to 30S ribosomal subunits. FEBS Lett. 1975 Nov 15;59(2):287–290. doi: 10.1016/0014-5793(75)80394-2. [DOI] [PubMed] [Google Scholar]
  489. van Wezenbeek P., Schoenmakers J. G. Nucleotide sequence of the genes III, VI and I of bacteriophage M13. Nucleic Acids Res. 1979 Jun 25;6(8):2799–2818. doi: 10.1093/nar/6.8.2799. [DOI] [PMC free article] [PubMed] [Google Scholar]
  490. van der Hofstad G. A., Buitenhek A., Bosch L., Voorma H. O. Initiation factor IF-3 and the binary complex between initiation factor IF-2 and formylmethionyl-tRNA are mutually exclusive on the 30-S ribosomal subunit. Eur J Biochem. 1978 Aug 15;89(1):213–220. doi: 10.1111/j.1432-1033.1978.tb20915.x. [DOI] [PubMed] [Google Scholar]
  491. van der Hofstad G. A., Buitenhek A., van den Elsen P. J., Voorma H. O., Bosch L. Binding of labeled initiation factor IF-1 to ribosomal particles and the relationship to the mode of IF-1 action in ribosome dissociation. Eur J Biochem. 1978 Aug 15;89(1):221–228. doi: 10.1111/j.1432-1033.1978.tb20916.x. [DOI] [PubMed] [Google Scholar]
  492. van der Hofstad G. A., Foekens J. A., Bosch L., Voorma H. O. The involvement of a complex between formylmethionyl-tRNA and initiation factor IF-2 in prokaryotic initiation. Eur J Biochem. 1977 Jul 1;77(1):69–75. doi: 10.1111/j.1432-1033.1977.tb11642.x. [DOI] [PubMed] [Google Scholar]