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.

  • Letters to Editor
  • Published:

Structural and Functional Evidence for a Repeated 50S Subunit Ribosomal Protein

Nature New Biology volume 242, pages 47–49 (1973)Cite this article

A Corrigendum to this article was published on 22 August 1973

Abstract

THE 50S ribosomal subunit of E. coli contains two acidic proteins with almost identical amino-acid sequences1–4. These two proteins differ apparently only in their N-terminal amino-acids: L7 begins with N-acetyl serine, while L12 begins with a free serine5. Either L7 or L12 must be present in the 50S subunit for the expression of G factor mediated GTPase activity6, which suggests a role for these proteins in translocation. They are the only proteins in the 50S subunit whose functions have been identified so far.

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

Access options

Buy this article

  • Purchase on Springer Link
  • Instant access to full article PDF
Buy now

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

References

  1. Kaltschmidt, E., and Wittmann, H. G., Proc. US Nat. Acad. Sci., 67, 1276 (1970).

    Article  CAS  Google Scholar 

  2. Mora, G., Donner, D., Thammana, P., Lutter, L., and Kurland, C. G., Mol. Gen. Genetics, 112, 229 (1971).

    CAS  Google Scholar 

  3. Stöffler, G., and Wittmann, H. G., J. Mol. Biol., 62, 407 (1971).

    Article  Google Scholar 

  4. Möller, W., Groene, A., Terhorst, C., and Amons, R., Europ. J. Biochem., 25, 5 (1972).

    Article  Google Scholar 

  5. Terhorst, C., Wittmann-Liebold, B., and Möller, W., Europ. J. Biochem., 25, 13 (1972).

    Article  CAS  Google Scholar 

  6. Kischa, K., Möller, W., and Stöffler, G., Nature, 233, 62 (1971).

    Article  CAS  Google Scholar 

  7. Voynow, P., and Kurland, C. G., Biochemistry, 10, 517 (1971).

    Article  CAS  Google Scholar 

  8. Weber, H. J., Molec. Gen. Genetics (in the press).

  9. Dzionara, M., Kaltschmidt, E., and Wittmann, H. G., Proc. US Nat. Acad. Sci., 67, 1909 (1970).

    Article  CAS  Google Scholar 

  10. Deusser, E., Mol. Gen. Genetics (in the press).

  11. Stöffler, G., and Wittmann, H. G., Proc. US Nat. Acad. Sci., 68, 2283 (1971).

    Article  Google Scholar 

  12. Stöffler, G., and Wittmann, H. G., J. Mol. Biol., 62, 407 (1971).

    Article  Google Scholar 

Download references

Author information

Author notes

  1. P. THAMMANA

    Present address: Department of Biochemistry, University of Wisconsin, Madison, Wisconsin

Authors and Affiliations

  1. Department of Molecular Biology, The Wallenberg Laboratory, University of Uppsala, Uppsala

    P. THAMMANA & C. G. KURLAND

  2. Max Planck Institut für Molekulare Genetik, Berlin-Dahlem

    E. DEUSSER, J. WEBER, R. MASCHLER, G. STÖFFLER & H. G. WITTMANN

Authors
  1. P. THAMMANA
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. C. G. KURLAND
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. E. DEUSSER
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. J. WEBER
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. R. MASCHLER
    View author publications

    You can also search for this author in PubMed Google Scholar

  6. G. STÖFFLER
    View author publications

    You can also search for this author in PubMed Google Scholar

  7. H. G. WITTMANN
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

THAMMANA, P., KURLAND, C., DEUSSER, E. et al. Structural and Functional Evidence for a Repeated 50S Subunit Ribosomal Protein. Nature New Biology 242, 47–49 (1973). https://doi.org/10.1038/newbio242047a0

Download citation

  • Received:

  • Revised:

  • Issue Date:

  • DOI: https://doi.org/10.1038/newbio242047a0

This article is cited by

Search

Advanced 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