Structural requirements for aminoacylation of Escherichia coli formylmethionine transfer RNA (original) (raw)

ArticleSeptember 1, 1977

Structural requirements for aminoacylation of Escherichia coli formylmethionine transfer RNA

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Biochemistry

Cite this: Biochemistry 1977, 16, 19

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Published September 1, 1977

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This article is cited by 30 publications.

  1. Naohiro Terasaka. General Introduction. 2017, 1-12. https://doi.org/10.1007/978-4-431-56517-8_1
  2. Naohiro Terasaka. Orthogonal Ribosome–tRNAs Pair by Engineering of Peptidyl Transferase Center. 2017, 43-81. https://doi.org/10.1007/978-4-431-56517-8_3
  3. Jennifer Shepherd, Michael Ibba. Bacterial transfer RNAs. FEMS Microbiology Reviews 2015, 39 (3) , 280-300. https://doi.org/10.1093/femsre/fuv004
  4. Naohiro Terasaka, Yoshihiko Iwane, Anna-Skrollan Geiermann, Yuki Goto, Hiroaki Suga. Recent Developments of Engineered Translational Machineries for the Incorporation of Non-Canonical Amino Acids into Polypeptides. International Journal of Molecular Sciences 2015, 16 (3) , 6513-6531. https://doi.org/10.3390/ijms16036513
  5. Naohiro Terasaka, Gosuke Hayashi, Takayuki Katoh, Hiroaki Suga. An orthogonal ribosome-tRNA pair via engineering of the peptidyl transferase center. Nature Chemical Biology 2014, 10 (7) , 555-557. https://doi.org/10.1038/nchembio.1549
  6. Leo Pallanck, Marie Pak, LaDonne H. Schulman. tRNA Discrimination in Aminoacylation. 2014, 371-394. https://doi.org/10.1128/9781555818333.ch18
  7. SHUYA FUKAI, OSAMU NUREKI, SHUN-ICHI SEKINE, ATSUSHI SHIMADA, DMITRY G. VASSYLYEV, SHIGEYUKI YOKOYAMA. Mechanism of molecular interactions for tRNA Val recognition by valyl-tRNA synthetase. RNA 2003, 9 (1) , 100-111. https://doi.org/10.1261/rna.2760703
  8. B Senger, F Fasiolo. Yeast tRNAMet recognition by methionyl-tRNA synthetase requires determinants from the primary, secondary and tertiary structure: a review. Biochimie 1996, 78 (7) , 597-604. https://doi.org/10.1016/S0300-9084(96)80006-X
  9. K. Tamura, N. Nameki, T. Hasegawa, M. Shimizu, H. Himeno. Role of the CCA terminal sequence of tRNA(Val) in aminoacylation with valyl-tRNA synthetase.. Journal of Biological Chemistry 1994, 269 (35) , 22173-22177. https://doi.org/10.1016/S0021-9258(17)31772-6
  10. Margaret E. Saks, Jeffrey R. Sampson, John N. Abelson. The Transfer RNA Identity Problem: a Search for Rules. Science 1994, 263 (5144) , 191-197. https://doi.org/10.1126/science.7506844
  11. O Nureki, T Muramatsu, K Suzuki, D Kohda, H Matsuzawa, T Ohta, T Miyazawa, S Yokoyama. Methionyl-tRNA synthetase gene from an extreme thermophile, Thermus thermophilus HB8. Molecular cloning, primary-structure analysis, expression in Escherichia coli, and site-directed mutagenesis.. Journal of Biological Chemistry 1991, 266 (5) , 3268-3277. https://doi.org/10.1016/S0021-9258(18)49984-X
  12. Véronique Perret, Catherine Florentz, Richard Giegé. Efficient aminoacylation of a yeast tRNA Asp transcript with a 5' extension. FEBS Letters 1990, 270 (1-2) , 4-8. https://doi.org/10.1016/0014-5793(90)81221-9
  13. LaDonne H. Schulman, Heike Pelka. The Anticodon Contains a Major Element of the Identity of Arginine Transfer RNAs. Science 1989, 246 (4937) , 1595-1597. https://doi.org/10.1126/science.2688091
  14. Anne THEOBALD, Mathias SPRINGER, Marianne GRUNBERG‐MANAGO, Jean‐Pierre EBEL, Richard GIEGE. Tertiary structure of Escherichia coli tRNA Thr 3 in solution and interaction of this tRNA with the cognate threonyl‐tRNA synthetase. European Journal of Biochemistry 1988, 175 (3) , 511-524. https://doi.org/10.1111/j.1432-1033.1988.tb14223.x
  15. David C. H. Yang, Blair Q. Ferguson. Conformational Dynamics in RNA—Protein Interactions: Immobilization of the Functional Domains in tRNAfMet and Methionyl-tRNA Synthetase. 1988, 71-76. https://doi.org/10.1007/978-1-4612-3744-0_9
  16. Laurence Marechal, Pierre Guillemaut, Jean-Michel Grienenberger, Genevi�ve Jeannin, Jacques-Henry Weil. Sequences of initiator and elongator methionine tRNAs in bean mitochondria. Plant Molecular Biology 1986, 7 (4) , 245-253. https://doi.org/10.1007/BF00752898
  17. Eric J. Ackerman, Andrzej Joachimiak, Vered Klinghofer, Paul B. Sigler. Directly photocrosslinked nucleotides joining transfer RNA to aminoacyl-tRNA synthetase in methionine and tyrosine systems. Journal of Molecular Biology 1985, 181 (1) , 93-102. https://doi.org/10.1016/0022-2836(85)90327-4
  18. Harald PAULSEN, Wolfgang WINTERMEYER. Incorporation of 1, N 6 ‐ethanoadenosine into the 3′ terminus of tRNA using T4 RNA ligase 1. Preparation of yeast tRNA Phe derivatives. European Journal of Biochemistry 1984, 138 (1) , 117-123. https://doi.org/10.1111/j.1432-1033.1984.tb07889.x
  19. Michael W. Gray, David F. Spencer. Wheat mitochondrial DNA encodes a eubacteria‐like initiator methionine transfer RNA. FEBS Letters 1983, 161 (2) , 323-327. https://doi.org/10.1016/0014-5793(83)81034-5
  20. Arthur E. Johnson, Harvey J. Adkins, Elizabeth A. Matthews, Charles R. Cantor. Distance moved by transfer RNA during translocation from the A site to the P site on the ribosome. Journal of Molecular Biology 1982, 156 (1) , 113-140. https://doi.org/10.1016/0022-2836(82)90462-4
  21. C. Zelwer, J.L. Risler, S. Brunie. Crystal structure of Escherichia coli methionyl-tRNA synthetase at 2.5 Å resolution. Journal of Molecular Biology 1982, 155 (1) , 63-81. https://doi.org/10.1016/0022-2836(82)90492-2
  22. Philippe Dessen, Guy Fayat, Giuseppe Zaccai, Sylvain Blanquet. Neutron-scattering studies of the binding of initiator tRNAMet to Escherichia coli trypsin-modified methionyl-tRNA synthetase. Journal of Molecular Biology 1982, 154 (4) , 603-613. https://doi.org/10.1016/S0022-2836(82)80017-X
  23. V.Sh. Scheinker, S.F. Beresten, T.D. Mashkova, A.M. Mazo, L.L. Kisselev. Role of exposed cytosine residues in aminoacylation activity of tRNA Trp. FEBS Letters 1981, 132 (2) , 349-352. https://doi.org/10.1016/0014-5793(81)81195-7
  24. S Yamashiro-Matsumura, M Kawata. Methionyl-tRNA synthetase-induced conformational change of Escherichia coli tRNAfMet.. Journal of Biological Chemistry 1981, 256 (17) , 9308-9312. https://doi.org/10.1016/S0021-9258(19)52547-9
  25. D. G. Knorre, V. V. Vlassov. Structural and Dynamic Aspects of Recognition Between tRNAs and Aminoacyl-tRNA Synthetases. 1980, 278-300. https://doi.org/10.1007/978-3-642-81503-4_22
  26. T. D. Mashkova, A. M. Mazo, V. Sh. Scheinker, S. F. Beresten, S. L. Bogdanova, T. A. Avdonina, L. L. Kisselev. A rapid method for mapping exposed cytosines in polyribonucleotides. Application to tRNATrp (yeast, beef liver). Molecular Biology Reports 1980, 6 (2) , 83-87. https://doi.org/10.1007/BF00778434
  27. D.G. Knorre, L.L. Kisselev. AMINOACYL-tRNA SYNTHETASES: APPROACHES TO THE STRUCTURE AND FUNCTION OF THE ACTIVE CENTERS. 1980, 315-325. https://doi.org/10.1016/B978-0-08-023967-5.50042-5
  28. Paul R. Schimmel, Ladonne Schulman. Five Specific Protein-Transfer RNA Interaction. Critical Reviews in Biochemistry 1980, 9 (3) , 207-251. https://doi.org/10.3109/10409238009105435
  29. Scott A. Reines, LaDonne H. Schulman. [7]A new method for attachment of fluorescent probes to tRNA. 1979, 146-156. https://doi.org/10.1016/0076-6879(79)59076-4
  30. W.J. Krzyżosiak, J. Biernat, J. Ciesiołka, P. Górnicki, M. Wiewiórowski. The reactions of thiouracils and thiouridines with chloroacetaldehyde. Tetrahedron Letters 1979, 20 (28) , 2647-2648. https://doi.org/10.1016/S0040-4039(01)86374-7

Biochemistry

Cite this: Biochemistry 1977, 16, 19

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Published September 1, 1977

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