Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

  • Letter
  • Published:

Ribosome slowed by mutation to streptomycin resistance

Abstract

ALTHOUGH the basic mechanisms of protein synthesis are now rather well understood, particularly in Escherichia coli, it is less clear how the high accuracy of this process is achieved. (The error rate in protein synthesis in E. coli seems to be about one in 104 amino acid misincorporations (Edelman and Gallant, unpublished results, and our own unpublished data)). A major site determining accuracy in protein synthesis is the ribosome, and in addition to the ribosome-mediated effects on accuracy (in vivo and in vitro) of various metal ions, aminoglycoside antibiotics and organic solvents, there are ribosomal mutations which increase or decrease accuracy2. Certain mutations of the 30S ribosomal protein SI2 conferring streptomycin resistance (the strA locus) enhance accuracy3–5, whereas certain mutations in the S4 protein (the ram locus) are known to decrease accuracy6. The strA mutations are restrictive (reducing) in their effect on both missense and nonsense suppression in vivo and on miscoding in vitro3, the ram mutation, on the other hand, has the opposite effect in both cases6. It is possible that it is the kinetics of polypeptide synthesis at the ribosome that determines accuracy and that the kinetics in turn are affected by the strA and ram mutations. Because the same transfer RNA (tRNA) discrimination kinetics that may determine accuracy may also contribute to the elongation speed, we have investigated the effect of mutation to streptomycin resistance on the speed of polypeptide elongation.

This is a preview of subscription content, access via your institution

Access options

Rent or buy this article

Prices vary by article type

from$1.95

to$39.95

Prices may be subject to local taxes which are calculated during checkout

Similar content being viewed by others

References

  1. Loftfield, R. B., Biochem. J., 89, 82–92 (1963).

    Article  CAS  Google Scholar 

  2. Gorini, L., and Davies, J., Curr. Top. Microbiol. Immun., 44, 100–122 (1968).

    CAS  Google Scholar 

  3. Gorini, L., and Kataja, E., Proc. natn. Acad. Sci. U.S.A., 51, 487 (1964).

    Article  ADS  CAS  Google Scholar 

  4. Gorini, L., Cold Spring Harb. Symp. quant. Biol., 31, 101–111 (1969).

    Article  Google Scholar 

  5. Gorini, L., Nature new Biol., 234, 261–264 (1972).

    Article  Google Scholar 

  6. Rosset, R., and Gorini, L., J. molec. Biol., 39, 95–112 (1969).

    Article  CAS  Google Scholar 

  7. Ninio, J., J. molec. Biol., 84, 297–313 (1974).

    Article  CAS  Google Scholar 

  8. Kepes, A., and Bequin, S., Biochim. biophys. Acta, 123, 546–560. (1966).

    Article  CAS  Google Scholar 

  9. Lacroute, F., and Stent, G. S., J. molec. Biol., 35, 165–173 (1968).

    Article  CAS  Google Scholar 

  10. Kepes, A., Biochim. biophys. Acta. 76, 293–309 (1963).

    Article  CAS  Google Scholar 

  11. Ozaki, M., Mizushima, S., Nomura, M., Nature, 222, 333–339 (1969).

    Article  ADS  CAS  Google Scholar 

  12. Leive, L., Biochem. biophys. Res. Commun., 20, 321–327 (1965).

    Article  CAS  Google Scholar 

  13. Perlman, R., and Pastan, I., Biochem. biophys. Res. Commun., 30, 656–664 (1968).

    Article  CAS  Google Scholar 

  14. Gupta, R., and Schlessinger, D., J. Bact., 125, 84–93 (1976).

    CAS  PubMed  Google Scholar 

  15. Zabin, I., and Fowler, A. V., in The Lactose Operon (edit. by Beckwith, J. R., and Zipser, D.) (Cold Spring Harbor Laboratory, New York, 1970).

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

GALAS, D., BRANSCOMB, E. Ribosome slowed by mutation to streptomycin resistance. Nature 262, 617–619 (1976). https://doi.org/10.1038/262617b0

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1038/262617b0

This article is cited by

Comments

By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.

Search

Quick links

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing