Cloning, structure, and expression of the Escherichia coli K-12 hisC gene (original) (raw)

Abstract

We used an expression vector plasmid containing the Escherichia coli K-12 histidine operon regulatory region to subclone the E. coli hisC gene. Analysis of plasmid-coded proteins showed that hisC was expressed in minicells. A protein with an apparent molecular weight of 38,500 was identified as the primary product of the hisC gene. Expression was under control of the hisGp promoter and resulted in very efficient synthesis (over 100-fold above the wild-type levels) of imidazolylacetolphosphate:L-glutamate aminotransferase, the hisC gene product. The complete nucleotide sequence of the hisC gene has been determined. The gene is 1,071 nucleotides long and codes for a protein of 356 amino acids with only one histidine residue.

1317

Images in this article

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Adams C. W., Hatfield G. W. Effects of promoter strengths and growth conditions on copy number of transcription-fusion vectors. J Biol Chem. 1984 Jun 25;259(12):7399–7403. [PubMed] [Google Scholar]
  2. Artz S., Holzschu D., Blum P., Shand R. Use of M13mp phages to study gene regulation, structure and function: cloning and recombinational analysis of genes of the Salmonella typhimurium histidine operon. Gene. 1983 Dec;26(2-3):147–158. doi: 10.1016/0378-1119(83)90184-1. [DOI] [PubMed] [Google Scholar]
  3. Atkins J. F., Loper J. C. Transcription initiation in the histidine operon of Salmonella typhimurium. Proc Natl Acad Sci U S A. 1970 Apr;65(4):925–932. doi: 10.1073/pnas.65.4.925. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Bachmann B. J. Linkage map of Escherichia coli K-12, edition 7. Microbiol Rev. 1983 Jun;47(2):180–230. doi: 10.1128/mr.47.2.180-230.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Barnes W. M. Cloning and restriction map of the first part of the histidine operon of Salmonella typhimurium. J Bacteriol. 1981 Jul;147(1):124–134. doi: 10.1128/jb.147.1.124-134.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Barnes W. M. DNA sequence from the histidine operon control region: seven histidine codons in a row. Proc Natl Acad Sci U S A. 1978 Sep;75(9):4281–4285. doi: 10.1073/pnas.75.9.4281. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Bhaduri S., Kasai T., Schlessinger D., Raskas H. J. pMB9 plasmids bearing the Salmonella typhimurium his operon and gnd gene. Gene. 1980 Feb;8(3):239–253. doi: 10.1016/0378-1119(80)90002-5. [DOI] [PubMed] [Google Scholar]
  8. Bickle T. A., Pirrotta V., Imber R. A simple, general procedure for purifying restriction endonucleases. Nucleic Acids Res. 1977 Aug;4(8):2561–2572. doi: 10.1093/nar/4.8.2561. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Bitar K. G., Firca J. R., Loper J. C. Histidinol dehydrogenase from salmonella typhimurium and Escherichia coli. Purification, some characteristics and the amino acid sequence around a reactive thiol group. Biochim Biophys Acta. 1977 Aug 23;493(2):429–440. doi: 10.1016/0005-2795(77)90199-4. [DOI] [PubMed] [Google Scholar]
  10. Blasi F., Bruni C. B. Regulation of the histidine operon: translation-controlled transcription termination (a mechanism common to several biosynthetic operons). Curr Top Cell Regul. 1981;19:1–45. doi: 10.1016/b978-0-12-152819-5.50018-x. [DOI] [PubMed] [Google Scholar]
  11. Bolivar F., Rodriguez R. L., Betlach M. C., Boyer H. W. Construction and characterization of new cloning vehicles. I. Ampicillin-resistant derivatives of the plasmid pMB9. Gene. 1977;2(2):75–93. doi: 10.1016/0378-1119(77)90074-9. [DOI] [PubMed] [Google Scholar]
  12. Bonner W. M., Laskey R. A. A film detection method for tritium-labelled proteins and nucleic acids in polyacrylamide gels. Eur J Biochem. 1974 Jul 1;46(1):83–88. doi: 10.1111/j.1432-1033.1974.tb03599.x. [DOI] [PubMed] [Google Scholar]
  13. Bruni C. B., Musti A. M., Frunzio R., Blasi F. Structural and physiological studies of the Escherichia coli histidine operon inserted into plasmid vectors. J Bacteriol. 1980 Apr;142(1):32–42. doi: 10.1128/jb.142.1.32-42.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Carlomagno M. S., Blasi F., Bruni C. B. Gene organization in the distal part of the Salmonella typhimurium histidine operon and determination and sequence of the operon transcription terminator. Mol Gen Genet. 1983;191(3):413–420. doi: 10.1007/BF00425756. [DOI] [PubMed] [Google Scholar]
  15. Clewell D. B. Nature of Col E 1 plasmid replication in Escherichia coli in the presence of the chloramphenicol. J Bacteriol. 1972 May;110(2):667–676. doi: 10.1128/jb.110.2.667-676.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Di Nocera P. P., Blasi F., Di Lauro R., Frunzio R., Bruni C. B. Nucleotide sequence of the attenuator region of the histidine operon of Escherichia coli K-12. Proc Natl Acad Sci U S A. 1978 Sep;75(9):4276–4280. doi: 10.1073/pnas.75.9.4276. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Ely B., Ciesla Z. Internal promoter P2 of the histidine operon of Salmonella typhimurium. J Bacteriol. 1974 Nov;120(2):984–986. doi: 10.1128/jb.120.2.984-986.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Fink G. R., Martin R. G. Translation and polarity in the histidine operon. II. Polarity in the histidine operon. J Mol Biol. 1967 Nov 28;30(1):97–107. doi: 10.1016/0022-2836(67)90246-x. [DOI] [PubMed] [Google Scholar]
  19. Frunzio R., Bruni C. B., Blasi F. In vivo and in vitro detection of the leader RNA of the histidine operon of Escherichia coli K-12. Proc Natl Acad Sci U S A. 1981 May;78(5):2767–2771. doi: 10.1073/pnas.78.5.2767. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Gouy M., Gautier C. Codon usage in bacteria: correlation with gene expressivity. Nucleic Acids Res. 1982 Nov 25;10(22):7055–7074. doi: 10.1093/nar/10.22.7055. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Grisolia V., Carlomagno M. S., Bruni C. B. Cloning and expression of the distal portion of the histidine operon of Escherichia coli K-12. J Bacteriol. 1982 Aug;151(2):692–700. doi: 10.1128/jb.151.2.692-700.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Grisolia V., Riccio A., Bruni C. B. Structure and function of the internal promoter (hisBp) of the Escherichia coli K-12 histidine operon. J Bacteriol. 1983 Sep;155(3):1288–1296. doi: 10.1128/jb.155.3.1288-1296.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Hershfield V., Boyer H. W., Yanofsky C., Lovett M. A., Helinski D. R. Plasmid ColEl as a molecular vehicle for cloning and amplification of DNA. Proc Natl Acad Sci U S A. 1974 Sep;71(9):3455–3459. doi: 10.1073/pnas.71.9.3455. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Johnston H. M., Barnes W. M., Chumley F. G., Bossi L., Roth J. R. Model for regulation of the histidine operon of Salmonella. Proc Natl Acad Sci U S A. 1980 Jan;77(1):508–512. doi: 10.1073/pnas.77.1.508. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. 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]
  26. Johnston H. M., Roth J. R. Genetic analysis of the histidine operon control region of Salmonella typhimurium. J Mol Biol. 1981 Feb 5;145(4):713–734. doi: 10.1016/0022-2836(81)90311-9. [DOI] [PubMed] [Google Scholar]
  27. Kasai T. Regulation of the expression of the histidine operon in Salmonella typhimurium. Nature. 1974 Jun 7;249(457):523–527. doi: 10.1038/249523a0. [DOI] [PubMed] [Google Scholar]
  28. Kleckner N., Roth J., Botstein D. Genetic engineering in vivo using translocatable drug-resistance elements. New methods in bacterial genetics. J Mol Biol. 1977 Oct 15;116(1):125–159. doi: 10.1016/0022-2836(77)90123-1. [DOI] [PubMed] [Google Scholar]
  29. Kohno T., Gray W. R. Chemical and genetic studies on L-histidinol dehydrogenase of Salmonella typhimurium. Isolation and structure of the tryptic peptides. J Mol Biol. 1981 Apr 15;147(3):451–464. doi: 10.1016/0022-2836(81)90495-2. [DOI] [PubMed] [Google Scholar]
  30. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  31. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  32. Loper J. C. Histidinol dehydrogenase from Salmonella typhimurium. Crystallization and composition studies. J Biol Chem. 1968 Jun 25;243(12):3264–3272. [PubMed] [Google Scholar]
  33. Margolies M. N., Goldberger R. F. Isolation of the fourth (isomerase) of histidine biosynthesis from Salmonella typhimurium. J Biol Chem. 1966 Jul 25;241(14):3262–3269. [PubMed] [Google Scholar]
  34. Margolies M. N., Goldberger R. F. Physical and chemical characterization of the isomerase of histidine biosynthesis in Salmonella typhimurium. J Biol Chem. 1967 Jan 25;242(2):256–264. [PubMed] [Google Scholar]
  35. Martin R. G., Goldberger R. F. Imidazolylacetolphosphate:L-glutamate aminotransferase. Purification and physical properties. J Biol Chem. 1967 Mar 25;242(6):1168–1174. [PubMed] [Google Scholar]
  36. Martin R. G. Imidazolylacetolphosphate: L-glutamate aminotransferase-mechanism of action. Arch Biochem Biophys. 1970 May;138(1):239–244. doi: 10.1016/0003-9861(70)90304-8. [DOI] [PubMed] [Google Scholar]
  37. Martin R. G., Silbert D. F., Smith W. E., Whitfield H. J., Jr Polarity in the histidine operon. J Mol Biol. 1966 Nov 14;21(2):357–369. doi: 10.1016/0022-2836(66)90104-5. [DOI] [PubMed] [Google Scholar]
  38. Martin R. G., Voll M. J., Appella E. Imidazolylacetolphosphate:L-glutamate aminotransferase. Composition and substructure. J Biol Chem. 1967 Mar 25;242(6):1175–1181. [PubMed] [Google Scholar]
  39. Maxam A. M., Gilbert W. Sequencing end-labeled DNA with base-specific chemical cleavages. Methods Enzymol. 1980;65(1):499–560. doi: 10.1016/s0076-6879(80)65059-9. [DOI] [PubMed] [Google Scholar]
  40. 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]
  41. Piszkiewicz D., Tilley B. E., Rand-Meir T., Parsons S. M. Amino acid sequence of ATP phosphoribosyltransferase of Salmonella typhimurium. Proc Natl Acad Sci U S A. 1979 Apr;76(4):1589–1592. doi: 10.1073/pnas.76.4.1589. [DOI] [PMC free article] [PubMed] [Google Scholar]
  42. Rechler M. M., Bruni C. B., Martin R. G., Terry W. An intercistronic region in the histidine operon of Salmonella typhimurium. J Mol Biol. 1972 Aug 28;69(3):427–452. doi: 10.1016/0022-2836(72)90256-2. [DOI] [PubMed] [Google Scholar]
  43. Rechler M. M., Bruni C. B. Properties of a fused protein formed by genetic manipulation. Histidinol dehydrogenase-imidazolylacetol phosphate: L-glutamate aminotransferase. J Biol Chem. 1971 Mar 25;246(6):1806–1813. [PubMed] [Google Scholar]
  44. Riggs D., Artz S. The hisD-hisC gene border of the Salmonella typhimurium histidine operon. Mol Gen Genet. 1984;196(3):526–529. doi: 10.1007/BF00436203. [DOI] [PubMed] [Google Scholar]
  45. Sancar A., Hack A. M., Rupp W. D. Simple method for identification of plasmid-coded proteins. J Bacteriol. 1979 Jan;137(1):692–693. doi: 10.1128/jb.137.1.692-693.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  46. Sanderson K. E., Hartman P. E. Linkage map of Salmonella typhimurium, edition V. Microbiol Rev. 1978 Jun;42(2):471–519. doi: 10.1128/mr.42.2.471-519.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  47. Schmid M. B., Roth J. R. Internal promoters of the his operon in Salmonella typhimurium. J Bacteriol. 1983 Feb;153(2):1114–1119. doi: 10.1128/jb.153.2.1114-1119.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  48. 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]
  49. Sutcliffe J. G. Complete nucleotide sequence of the Escherichia coli plasmid pBR322. Cold Spring Harb Symp Quant Biol. 1979;43(Pt 1):77–90. doi: 10.1101/sqb.1979.043.01.013. [DOI] [PubMed] [Google Scholar]
  50. Thomas P. S. Hybridization of denatured RNA and small DNA fragments transferred to nitrocellulose. Proc Natl Acad Sci U S A. 1980 Sep;77(9):5201–5205. doi: 10.1073/pnas.77.9.5201. [DOI] [PMC free article] [PubMed] [Google Scholar]
  51. VOGEL H. J., BONNER D. M. Acetylornithinase of Escherichia coli: partial purification and some properties. J Biol Chem. 1956 Jan;218(1):97–106. [PubMed] [Google Scholar]
  52. Verde P., Frunzio R., di Nocera P. P., Blasi F., Bruni C. B. Identification, nucleotide sequence and expression of the regulatory region of the histidine operon of Escherichia coli K-12. Nucleic Acids Res. 1981 May 11;9(9):2075–2086. doi: 10.1093/nar/9.9.2075. [DOI] [PMC free article] [PubMed] [Google Scholar]
  53. Voll M. J., Appella E., Martin R. G. Purification and composition studies of phosphoribosyladenosine triphosphate:pyrophosphate phosphoribosyltransferase, the first enzyme of histidine biosynthesis. J Biol Chem. 1967 Apr 25;242(8):1760–1767. [PubMed] [Google Scholar]
  54. 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]
  55. Yourno J. Composition and subunit structure of histidinol dehydrogenase from Salmonella typhimurium. J Biol Chem. 1968 Jun 25;243(12):3277–3288. [PubMed] [Google Scholar]
  56. Yourno J., Kohno T., Roth J. R. Enzyme evolution: generation of a bifunctional enzyme by fusion of adjacent genes. Nature. 1970 Nov 28;228(5274):820–824. doi: 10.1038/228820a0. [DOI] [PubMed] [Google Scholar]