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:

Drosophila small cytoplasmic 19S ribonucleoprotein is homologous to the rat multicatalytic proteinase

Abstract

All eukaryotic cells so far analysed contain 19S particles which share a cylinder-like shape and are composed of a set of proteins of relative molecular mass ranging typically from 19,000 to 36,000 (refs 1–10). Proposed functions have included synthetase activity11, transfer RNA processing12 or messenger RNA repression6, but their biological importance remains obscure. A multicatalytic proteinase (MCP) of similar size and shape has been isolated from mammalian tissues13–24. The apparent similarities of these high molecular weight complexes suggest a biochemical and functional homology between the small cytoplasmic 19S particle from Drosophila melanogaster (19S-scRNP) (ref. 7) and rat MCP (ref. 14). By means of electron microscopy, immunological techniques, RNA identification and proteinase activity assays, we were able to show that the two structurally similar complexes are immunologically related ribonucleoproteins (RNPs) with similar proteolytic activity.

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

Access options

Buy this article

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

Similar content being viewed by others

References

  1. Kloetzel, P.-M. Molec. Biol. Rep. 12, 223–227 (1987).

    Article  Google Scholar 

  2. Domae, N. et al. Life Sci. 30, 469–477 (1981).

    Article  Google Scholar 

  3. Harmon, F. R., Spohn, W. H., Domae, N., Soo Ha, C. & Busch, H. Cell Biol. int. Rep. 7, 333–343 (1983).

    Article  CAS  Google Scholar 

  4. Kleinschmidt, J. A., Hügle, B., Grund, C. & Franke, W. W. Eur. J. cell Biol. 32, 143–156 (1983).

    CAS  PubMed  Google Scholar 

  5. Hügle, B., Kleinschmidt, J. A. & Franke, W. W. Eur. J. cell Biol. 32, 157–163 (1983).

    PubMed  Google Scholar 

  6. Schmid, H.-P. et al. EMBO J. 3, 29–34 (1984).

    Article  CAS  Google Scholar 

  7. Schuldt, C. & Kloetzel, P.-M. Devl Biol. 110, 65–74 (1985).

    Article  CAS  Google Scholar 

  8. Arrigo, A.-P., Darlix, J.-L., Khandjian, E. W., Simon, M. & Spahr, P.-F. EMBO J. 4, 399–406 (1985).

    Article  CAS  Google Scholar 

  9. Arrigo, A.-P. J. molec. Evol. 25, 141–150 (1987).

    Article  ADS  CAS  Google Scholar 

  10. de Sa, C. M. J. molec. Biol. 187, 479–493 (1986).

    Article  Google Scholar 

  11. Shelton, E., Kuff, E. L., Maxwell, E. S. & Harrington, J. T. J. cell Biol. 45, 1–8 (1970).

    Article  CAS  Google Scholar 

  12. Castaño, J., Ornberg, R., Koster, J. G., Tobian, J. A. & Zasloff, M. Cell 46, 377–387 (1986).

    Article  Google Scholar 

  13. Wilk, S. & Orlowski, M. J. Neurochem. 40, 842–849 (1983).

    Article  CAS  Google Scholar 

  14. Dahlmann, B., Kuehn, L., Rutschmann, M. & Reinauer, H. Biochem. J. 228, 161–170 (1985).

    Article  CAS  Google Scholar 

  15. Ray, K. & Harris, H. Proc. natn. Acad. Sci. U.S.A. 82, 7545–7549 (1985).

    Article  ADS  CAS  Google Scholar 

  16. Rivett, A. J. J. biol. Chem. 260, 12600–12606 (1985).

    CAS  PubMed  Google Scholar 

  17. Nojima, M. et al. J. Biochem., Tokyo 99, 1605–1611 (1986).

    Article  CAS  Google Scholar 

  18. Ishiura, S. & Sugita, H. J. Biochem., Tokyo 100, 753–763 (1986).

    Article  CAS  Google Scholar 

  19. McGuire, M. J. & De Martino, G. N. Biochem. biophys. Acta 873, 279–289 (1986).

    CAS  PubMed  Google Scholar 

  20. Yamamoto, T., Nojima, M., Ishiura, S. & Sugita, H. Biochem. biophys. Acta 882, 297–304 (1986).

    Article  CAS  Google Scholar 

  21. Tanaka, K., Ii, K., Ichihara, A., Waxman, L. & Goldberg, A. L. J. biol. Chem. 261, 15197–15203 (1986).

    CAS  PubMed  Google Scholar 

  22. Tanaka, K., Yoshimura, T., Ichihara, A., Kameyama, K. & Takagi, T. J. biol. Chem. 261, 15204–15207 (1986).

    CAS  PubMed  Google Scholar 

  23. Zolfaghari, R., Baker, C. R. F., Canizaro, P. C., Amirgholami, A. & Behal, F. J. Biochem. J. 241, 129–135 (1987).

    Article  CAS  Google Scholar 

  24. Hough, R., Pratt, G. & Rechsteiner, M. J. biol. Chem. 262, 8303–8313 (1987).

    CAS  PubMed  Google Scholar 

  25. Kopp, F., Steiner, R., Dahlmann, B., Kuehn, L. & Reinauer, H. Biochem. biophys. Acta 872, 253–260 (1986).

    CAS  PubMed  Google Scholar 

  26. Killary, A. M. & Fournier, R. E. K. Cell 38, 523–534 (1984).

    Article  CAS  Google Scholar 

  27. Kloetzel, P.-M., Falkenburg, P.-E., Hössl, P. & Glätzer, K. H. Expl Cell Res. 170, 204–213 (1987).

    Article  CAS  Google Scholar 

  28. Lämmli, U. K. Nature 227, 680–685 (1970).

    Article  ADS  Google Scholar 

  29. Kloetzel, P.-M., Johnson, R. M. & Sommerville, J. Eur. J. Biochem. 127, 301–308 (1982).

    Article  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Falkenburg, PE., Haass, C., Kloetzel, PM. et al. Drosophila small cytoplasmic 19S ribonucleoprotein is homologous to the rat multicatalytic proteinase. Nature 331, 190–192 (1988). https://doi.org/10.1038/331190a0

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1038/331190a0

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