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Elongation Cycle, Step I: Aminoacyl-tRNA Binding

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Ribosomes

Part of the book series: Cellular Organelles ((CORG))

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Abstract

Analysis of the elongation cycle may conveniently begin at the point when the peptidyl-tRNA occupies the P site of the translating ribosome while the A site with the codon of the template polynucleotide positioned there is vacant (Fig. 9.1, top). Such a ribosome is capable of binding the next aminoacyl-tRNA molecule.

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References

  • Bogosian, G., Violand, B. N., Jung, P. E., and Kane, J. F. (1990) Effect of protein overexpression on mistranslation in Escherichia coli, RR in The Ribosome: Structure, Function, and Evolution (W. E. Hill, A. Dahlberg, R. A. Garrett, P. B. Moore, D. Schlessinger, and J. R. Warner, eds.), pp. 546–558, ASM Press, Washington, DC.

    Google Scholar 

  • Chapeville, F., Lipmann, F., von Ehrenstein, G., Weisblum, B., Ray, W. J., and Benzer, S. (1962) On the role of soluble ribonucleic acid in coding for amino acids, Proc. Natl. Acad. Sci. USA 48:1086–1092.

    Article  PubMed  CAS  Google Scholar 

  • Coons, S. F., Smith, L. F., and Loftfield, R. B. (1979) The nature of amino acid errors in in vivo biosynthesis of rabbit hemoglobin, Fed. Proc. 38:328.

    Google Scholar 

  • Crick, F. H. C. (1966) Codon-anticodon pairing: The wobble hypothesis, J. Mol. Biol. 19:548–555.

    Article  PubMed  CAS  Google Scholar 

  • Cundliffe, E. (1980) Antibiotic and prokaryotic ribosomes: Action, interaction, and resistance, in Ribosomes: Structure, Function, and Genetics (G. Chambliss, G. R. Craven, J. Davies, K. Davis, L. Kahan, and M. Nomura, eds.), pp. 555–581, University Park Press, Baltimore.

    Google Scholar 

  • Cundliffe, E. (1990) Recognition sites for antibiotics within rRNA, in The Ribosome: Structure, Function, and Evolution (W. E. Hill, A. Dahlberg, R. A. Garrett, P. B. Moore, D. Schlessinger, and J. R. Warner, eds.), pp. 479–490, ASM Press, Washington.

    Google Scholar 

  • Davies, J. E., Gilbert, W., and Gorini, L. (1964) Streptomycin, suppression, and the code, Proc. Natl. Acad. Sci. USA 51:883–890.

    Article  PubMed  CAS  Google Scholar 

  • Davies, J. E., Gorini, L., and Davis, B. D. (1965) Misreading of RNA codewords induced by aminoglycoside antibiotics, J. Mol. Pharmacol. 1:93–106.

    CAS  Google Scholar 

  • Edelman, P., and Gallant, J. (1977) Mistranslation in E. coli, Cell 10:131–137.

    Article  Google Scholar 

  • Ehrenstein, von, G., Weisblum, B., and Benzer, S. (1963) The function of sRNA as amino acid adaptor in the synthesis of hemoglobin, Proc. Natl. Acad. Sci. USA 49:669–675.

    Article  PubMed  CAS  Google Scholar 

  • Fourmy, D., Recht, M. I., Blanchard, S., and Puglisi, J. D. (1996) Structure of the A site of Escherichia coli 16S ribosomal RNA complexed with an aminoglycoside antibiotic, Science 274:1367–1371.

    Article  PubMed  CAS  Google Scholar 

  • Gale, E. F., Cundliffe, E., Reynolds, P. E., Richmond, M. H., and Waring, M. J. (1981) The Molecular Basis of Antibiotic Action, John Wiley and Sons, London.

    Google Scholar 

  • Gallant, J. and Foley, D. (1979) On the causes and prevention of mistranslation, in Ribosomes: Structure, Function, and Genetics (G. Chambliss, G. R. Craven, J. Davies, K. Davis, L. Kahan, and M. Nomura, eds.), pp. 615–638, University Park Press, Baltimore.

    Google Scholar 

  • Goodman, H. M., Abelson, J., Landy, A., Brenner, S., and Smith, J. D. (1968) Amber suppression: A nucleotide change in the anticodon of a tyrosine transfer RNA, Nature 217:1019–1024.

    Article  PubMed  CAS  Google Scholar 

  • Gorini, L. (1971) Ribosomal discrimination of tRNAs, Nature New Biol. 234:264.

    Google Scholar 

  • Gorini, L. (1974) Streptomycin and misreading of the genetic code, in Ribosomes (M. Nomura, A. Tissières, and P. Lengyel, eds.), pp. 791–803, CSHL Press, Cold Spring Harbor, NY.

    Google Scholar 

  • Green, R., and Noller, H. F. (1997) Ribosomes and translation, Annu. Rev. Biochem. 66:679–716.

    Article  PubMed  CAS  Google Scholar 

  • Hopfield, J. J. (1974) Kinetic proofreading: A new mechanism for reducing errors in biosynthetic processes requiring high specificity, Proc. Natl. Acad. Sci. USA 71:4135–4139.

    Article  PubMed  CAS  Google Scholar 

  • Kurland, C. G., and Ehrenberg, M. (1984) Optimization of translation accuracy, Progr. Nucleic Acid Res. Mol. Biol. 31:191–219.

    Article  CAS  Google Scholar 

  • Kurland, C. G., Joergensen, F., Richter, A., Ehrenberg, M., Bilgin, N., and Rojas, A.-M. (1990) Through the accuracy window, in The Ribosome: Structure, Function, and Evolution (W. E. Hill, A. Dahlberg, R. A. Garrett, P. B. Moore, D. Schlessinger, and J. R. Warner, eds.), pp. 513–526, ASM Press, Washington, DC.

    Google Scholar 

  • Loftfield, R. B., and Vanderjagt, D. (1972) The frequency of errors in protein biosynthesis, Biochem. J. 128:1353–1356.

    PubMed  CAS  Google Scholar 

  • Merrick, W. C., and Hershey, J. W. B. (1996) The pathway and mechanism of eukaryotic protein synthesis, in Translational Control (J. W. B. Hershey, M. B. Mathews, and N. Sonenberg, eds.), pp. 31–69, CSHL Press, Cold Spring Harbor, NY.

    Google Scholar 

  • Ninio, J. (1974) A semi-quantitative treatment of missense and nonsense suppression in the strA and ram ribosomal mutants of Escherichia coli:RR Evaluation of some molecular parameters of translation in vivo, J. Mol. Biol. 84:297–313.

    Article  PubMed  CAS  Google Scholar 

  • Noller, H. F. (1991) Ribosomal RNA and translation, Annu. Rev. Biochem. 60:191–227.

    Article  PubMed  CAS  Google Scholar 

  • Noller, H. F., Moazed, D., Stern, S., Powers, T., Allen, P. N., Robertson, J. M., Weiser, B., and Triman, K. (1990) Structure of rRNA and its functional interactions in translation, in The Ribosome: Structure, Function, and Evolution (W. E. Hill, A. Dahlberg, R. A. Garrett, P. B. Moore, D. Schlessinger, and J. R. Warner, eds.), pp. 73–92 ASM Press, Washington, DC.

    Google Scholar 

  • Parker, J., Johnston, T. C., Borgia, P. T., Holtz, G., Remaut, E., and Fiers, W. (1983) Codon usage and mistranslation. In vivo basal level misreading of the MS2 coat protein message, J. Biol. Chem. 258:10007–10012.

    PubMed  CAS  Google Scholar 

  • Parker, J., Pollard, J. W., Friesen, J. D., and Stanners, C. P. (1978) Shuttering: High-level mistranslation in animal and bacterial cells, Proc. Natl. Acad. Sci. USA 75:1091–1095.

    Article  PubMed  CAS  Google Scholar 

  • Pestka, S. (1977) Inhibitors of protein synthesis, in Molecular Mechanisms of Protein Biosynthesis (H. Weissbach and S. Pestka, eds.), pp. 467–555, Academic Press, New York.

    Google Scholar 

  • Pirohit, P., and Stern, S. (1994) Interactions of a small RNA with antibiotics and RNA ligands of the 30S subunit. Nature 370:659–662.

    Article  Google Scholar 

  • Rodnina, M. V., Fricke, R., and Wintermeyer, W. (1993) Kinetic fluorescence study on EF-Tu-dependent binding of Phe-tRNAPhe to the ribosomal A site, in The Translational Apparatus (K. H. Nierhaus, F. Franceschi, A. R. Subramanian, V. A. Erdmann, and B. Wittmann-Liebold, eds.), pp. 317–326, Plenum Press, New York.

    Chapter  Google Scholar 

  • Yokoyama, S., and Nishimura, S. (1995) Modified nucleosides and codon recognition, in tRNA: Structure, Biosynthesis, and Function (D. Soell and U. L. RajBhandary, eds.), pp. 207–223, ASM Press, Washington, DC.

    Google Scholar 

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Authors and Affiliations

  1. Russian Academy of Sciences, Moscow, Russia

    Alexander S. Spirin

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  1. Alexander S. Spirin
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© 1999 Kluwer Academic/Plenum Publishers, New York

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Spirin, A.S. (1999). Elongation Cycle, Step I: Aminoacyl-tRNA Binding. In: Ribosomes. Cellular Organelles. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-7817-8_10

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  • DOI: https://doi.org/10.1007/978-1-4615-7817-8_10

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-0-306-46146-0

  • Online ISBN: 978-1-4615-7817-8

  • eBook Packages: Springer Book Archive

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