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:

A kinase–cyclin pair in the RNA polymerase II holoenzyme

Abstract

THE RNA polymerase II holoenzyme consists of RNA polymerase II, a subset of general transcription factors, and regulatory proteins known as SRB proteins1,2. The genes encoding SRB proteins were isolated as suppressors of mutations in the RNA polymerase II carboxy-terminal domain (CTD)3,4. The CTD and SRB proteins have been implicated in the response to transcriptional regulators1–11. We report here the isolation of two new SRB genes, SRB10 and SRB11, which encode kinase- and cyclin-like proteins, respectively. Genetic and biochemical evidence indicates that the SRB 10 and SRB 11 proteins form a kinase–cyclin pair in the holoenzyme. The SRB10/11 kinase is essential for a normal transcriptional response to galactose induction in vivo. Holoenzymes lacking SRB 10/11 kinase function are strikingly deficient in CTD phosphory lation. Although defects in the kinase substantially affect transcription in vivo, purified holoenzymes lacking SRB10/11 kinase function do not show defects in definedin vitro transcription systems, suggesting that the factors necessary to elicit the regulatory role of the SRB10/11 kinase are missing in these systems. These results indicate that the SRB 10/11 kinase is involved in CTD phosphorv lation and suggest that this modification has a role in the response to transcriptional regulators in vivo.

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. Koleske, A. J. & Young, R. A. Nature 368, 466–469 (1994).

    Article  ADS  CAS  Google Scholar 

  2. Kim, Y.-J., Bjorklund, S., Li, Y., Sayre, M. H. & Kornberg, R. D. Cell 77, 599–609 (1994).

    Article  CAS  Google Scholar 

  3. Koleske, A. J., Buratowski, S., Nonet, M. & Young, R. A. Cell 69, 883–894 (1992).

    Article  CAS  Google Scholar 

  4. Thompson, C. M., Koleske, A. J., Chao, D. M. & Young, R. A. Cell 73, 1361–1375 (1993).

    Article  CAS  Google Scholar 

  5. Allison, L. A. & Ingles, C. J. Proc. natn. Acad. Sci. U.S.A. 86, 2794–2798 (1989).

    Article  ADS  CAS  Google Scholar 

  6. Scafe, C. et al. Nature 347, 491–494 (1990).

    Article  ADS  CAS  Google Scholar 

  7. Peterson, C. L., Kruger, W. & Herskowitz, I. Cell 64, 1135–1143 (1991).

    Article  CAS  Google Scholar 

  8. Liao, S.-M., Taylor, I. C. A., Kingston, R. E. & Young, R. A. Genes Dev. 5, 2431–2440 (1991).

    Article  CAS  Google Scholar 

  9. Li, Y. & Kornberg, R. D. Proc. natn. Acad. Sci. U.S.A. 91, 2362–2366 (1994).

    Article  ADS  CAS  Google Scholar 

  10. Young, R. A. Rev. Biochem. 60, 689–715 (1991).

    Article  CAS  Google Scholar 

  11. Dahmus, M. E. & Dynan, W. S. in Transcriptional Regulation 109–128 (Cold Spring Harbor Laboratory Press, Cold Spring Harbor, 1992).

    Google Scholar 

  12. Lorincz, A. T. & Reed, S. I. Nature 307, 183–185 (1984).

    Article  ADS  CAS  Google Scholar 

  13. Surosky, R. T., Strich, R. & Esposito, R. E. Molec. cell. Biol. 13, 3446–3458 (1994).

    Article  Google Scholar 

  14. Uesono, Y., Tanka, K. & Toh-e, A. Nucleic Acids Res. 15, 10299–10309 (1987).

    Article  CAS  Google Scholar 

  15. Lees, J. M. & Greenleaf, A. L. Gene Expr. 1, 149–167 (1991).

    Google Scholar 

  16. Simon, M., Seraphin, B. & Faye, G. EMBO J. 5, 2697–2701 (1986).

    Article  CAS  Google Scholar 

  17. Lew, D. J., Dulic, V. & Reed, S. I. Cell 66, 1197–1206 (1991).

    Article  CAS  Google Scholar 

  18. Leopold, P. & O'Farrell, P. H. Cell 66, 1207–1216 (1991).

    Article  CAS  Google Scholar 

  19. Xiong, Y., Menninger, J., Beach, D. & Ward, D. C. Genomics 13, 575–584 (1992).

    Article  CAS  Google Scholar 

  20. Kobayashi, H. et al. Molec. Biol. Cell 3, 1279–1294 (1992).

    Article  CAS  Google Scholar 

  21. Lees, E. M. & Harlow, E. Molec. cell. Biol. 13, 1194–1201 (1993).

    Article  CAS  Google Scholar 

  22. Fields, S. & Song, O. Nature 340, 245–246 (1989).

    Article  ADS  CAS  Google Scholar 

  23. O'Brien, T., Hardin, S., Greenleaf, A. & Lis, J. T. Nature 370, 75–77 (1994).

    Article  ADS  CAS  Google Scholar 

  24. Feaver, W. J., Svejstrup, J. Q., Henry, N. L. & Kornberg, R. D. Cell 79, 1103–1110 (1994).

    Article  CAS  Google Scholar 

  25. Feaver, W. J., Gileadi, O., Li, Y. & Kornberg, R. Cell 67, 1223–1330 (1991).

    Article  CAS  Google Scholar 

  26. Kolodziej, P. & Young, R. A. Meth. Enzym. 194, 508–519 (1991).

    Article  CAS  Google Scholar 

  27. Smith, D. B. & Johnson, K. S. Gene 67, 31–40 (1988).

    Article  CAS  Google Scholar 

  28. Rothstein, R. Meth. Enzyme. 194, 281–301 (1991).

    Article  CAS  Google Scholar 

  29. Sayre, M. H., Tschochner, H. & Kornberg, R. D. J. biol. Chem. 267, 23383–23387 (1992).

    CAS  Google Scholar 

  30. Kim, T. K. et al. Nature 369, 252–255 (1994).

    Article  ADS  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Liao, SM., Zhang, J., Jeffery, D. et al. A kinase–cyclin pair in the RNA polymerase II holoenzyme. Nature 374, 193–196 (1995). https://doi.org/10.1038/374193a0

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1038/374193a0

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