Skip to main content
Log in

New aspects of the ribosomal elongation cycle

  • Original Articles
  • Published:
Molecular and Cellular Biochemistry Aims and scope Submit manuscript

Summary

The ribosomal elongation cycle represents a series of reactions during which the polypeptide is prolonged by one amino acid and after which the prolonged polypeptidyl residue is again ready to accept the next aminoacyl residue. It is generally believed that the ribosome carries two tRNA binding sites, the A site for aminoacyl-tRNA and the P site for peptidyl-tRNA, leading to the classical two-site model of the ribosome as a description for the elongation cycle. However, evidence is accumulating which is in conflict with the classical two-site model. These conflicts are resolved in a new three-site model which is discussed in detail in this paper.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

Abbreviations

AcPhe-tRNA:

N-acetyl-Phe-tRNA

References

  1. Watson, J. D., 1964. Bull. Soc. Chim. Biol. 46: 1399–1425.

    Google Scholar 

  2. Leder, P., 1973. Adv. Prot. Chem. 27: 213–242.

    Google Scholar 

  3. Nierhaus, K. H., 1982. Curr. Topics Microbiol. Immunol. 97: 81–155.

    Google Scholar 

  4. Rheinberger, H.-J. and Nierhaus, K. H., 1983. Proc. Natl. Acad. Sci. U.S.A. 80: 4213–4217.

    Google Scholar 

  5. Rheinberger, H.-J., Sternbach, H. and Nierhaus, K. H., 1981. Proc. Natl. Acad. Sci. U.S.A. 78: 5310–5314.

    Google Scholar 

  6. Rheinberger, H.-J. and Nierhaus, K. H., 1980. Biochem. Int. 1: 297–303.

    Google Scholar 

  7. Rheinberger, H.-J., Schilling, S. and Nierhaus, K. H., 1983. Eur. J. Biochem. 134: 421–428.

    Google Scholar 

  8. Kirillov, S. V. and Semenkov, Y. P., 1982. FEBS Lett. 148: 235–238.

    Google Scholar 

  9. Kirillov, S. V., Makhno, V. I. and Semenkov, Y. P., 1980. Nucl. Acids Res. 8: 183–196.

    Google Scholar 

  10. Wurmbach, P. and Nierhaus, K. H., 1979. Proc. Natl. Acad. Sci. U.S.A. 76: 2143–2147.

    Google Scholar 

  11. Wurmbach, P. and Nierhaus, K. H., 1983. Eur. J. Biochem. 130:9–12.

    Google Scholar 

  12. Wettstein, F. O. and Noll, H., 1965. J. Mol. Biol. 11: 35–53.

    Google Scholar 

  13. Weissbach, H., Redfield, B. and Brot, N., 1968. Arch. Biochem. Biophys. 127: 705–710.

    Google Scholar 

  14. De Groot, N., Panet, A. and Lapidot, Y., 1970. Eur. J. Biochem. 15: 215–221.

    Google Scholar 

  15. Klotz, I. M. and Hunston, D. L., 1979. Arch. Biochem. Biophys. 193: 314–328.

    Google Scholar 

  16. Schmitt, M., Neugebauer, U., Bergmann, C., Gassen, H. G. and Riesner, D., 1982. Eur. J. Biochem. 127: 525–529.

    Google Scholar 

  17. Infante, A. A. and Baierlein, R., 1971. Proc. Natl. Acad. Sci. U.S.A. 68: 1780–1785.

    Google Scholar 

  18. Dixon, M., Webb, E. C., Thorne, C. J. R. and Tripton, K. F., 1979. In: Enzymes, 3rd edn., pp. 399–405, Longman, London.

    Google Scholar 

  19. Grajevskaja, R. A., Ivanov, Y. V. and Saminsky, E. M., 1982. Eur. J. Biochem. 128: 47–52.

    Google Scholar 

  20. Holschuh, K., Bonin, J. and Gassen, H. G., 1980. Biochemistry 19: 5857–5864.

    Google Scholar 

  21. Holschuh, K. and Gassen, H. G., 1980. FEBS Lett. 110: 169–172.

    Google Scholar 

  22. Schmitt, M., Möller, A., Riesner, D. and Gassen, H. G., 1981. Eur. J. Biochem. 119: 61–66.

    Google Scholar 

  23. Holschuh, K., Riesner, D. and Gassen, H. G., 1981. Nature 293: 675–677.

    Google Scholar 

  24. Holschuh, K. and Gassen, H. G., 1982. J. Biol. Chem. 257: 1987–1992.

    Google Scholar 

  25. Shorey, R. L., Ravel, J. M. and Shive, W., 1971. Arch. Biochem. Biophys. 146: 110–117.

    Google Scholar 

  26. Szer, W. and Ochoa, S., 1964. J. Mol. Biol. 8: 823–834.

    Google Scholar 

  27. Gavrilova, L. P. and Ruthkevitch, N. M., 1980. FEBS Lett. 120: 135–140.

    Google Scholar 

  28. Modelell, J. and Davis, B. D., 1968. Proc. Natl. Acad. Sci. U.S.A. 61: 1279–1286.

    Google Scholar 

  29. Richter, D., 1976. Proc. Natl. Acad. Sci. U.S.A. 73: 707–711.

    Google Scholar 

  30. De Groot, N., Panet, A. and Lapidot, Y., 1971. Eur. J. Biochem. 23: 523–527.

    Google Scholar 

  31. Watanabe, S., 1972. J. Mol. Biol. 67: 443–457.

    Google Scholar 

  32. Ishitsuka, H., Kuriki, Y. and Kaji, A., 1970. J. Biol. Chem. 245: 3346–3351.

    Google Scholar 

  33. Inoue-Yokosawa, N., Ishikawa, C. and Kaziro, Y., 1974. J. Biol. Chem. 249: 4321–4323.

    Google Scholar 

  34. Lucas-Lenard, J. and Haenni, A.-L., 1969. Proc. Natl. Acad. Sci. U.S.A. 63: 93–97.

    Google Scholar 

  35. Modolell, J., Cabrer, B. and Vazquez, D., 1973. J. Biol. Chem. 248: 8356–8360.

    Google Scholar 

  36. Tanaka, N., Lin, Y.-C. and Okuyama, A., 1971. Biochem. Biophys. Res. Commun. 44: 477–483.

    Google Scholar 

  37. Tanaka, S. and Kaji, A., 1972. Biochem. Biophys. Res. Commun. 46: 136–142.

    Google Scholar 

  38. Belitsina, N. V., Glukova, M. A. and Spirin, A. S., 1979. Methods Enzymol. 60: 761–779.

    Google Scholar 

  39. Odinzov, V. B. and Kirillov, S. V., 1978. Nucl. Acids Res. 5: 3871–3879.

    Google Scholar 

  40. Tanaka, S. and Kaji, A., 1972. Biochem. Biophys. Res. Commun. 46: 136–142.

    Google Scholar 

  41. Bergemann, K. and Nierhaus, K. H., 1984. J. Biol. Chem. (in press).

  42. Pestka, S., 1969. J. Biol. Chem. 244: 1533–1539.

    Google Scholar 

  43. Gavrilova, L. P. and Spirin, A. S., 1974. Methods Enzymol. 30: 452–462.

    Google Scholar 

  44. Abdurashidova, G. G., Turchinsky, M. F. and Budowsky, E. I., 1981. FEBS Lett. 129: 59–61.

    Google Scholar 

  45. Abdurashidova, G. G., Turchinsky, M. F., Aslanov, K. A. and Budowsky, E. I., 1979. Nucl. Acids Res. 6: 3891–3909.

    Google Scholar 

  46. Warner, J. R. and Rich, A., 1963. Proc. Natl. Acad. Sci. U.S.A. 51: 1134–1141.

    Google Scholar 

  47. Riddle, D. L. and Carbon, J., 1973. Nature New Biol. 242: 230–234.

    Google Scholar 

  48. Belitsina, N. V., Tnalina, G. Z. and Spirin, A. S., 1981. FEBS Lett. 131: 289–292.

    Google Scholar 

  49. Belitsina, N. V., Tnalina, G. Z. and Spirin, A. S., 1982. BioSystems 15: 233–241.

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Nierhaus, K.H. New aspects of the ribosomal elongation cycle. Mol Cell Biochem 61, 63–81 (1984). https://doi.org/10.1007/BF00239606

Download citation

  • Received:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00239606

Keywords

Navigation