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 highly conserved ATPase protein as a mediator between acidic activation domains and the TATA-binding protein

Nature volume 374, pages 88–91 (1995)Cite this article

A Correction to this article was published on 15 February 1996

Abstract

BIOCHEMICAL and genetic studies suggest the existence of mediators that work between the activation domains (ADs) of regulatory proteins and the basic transcriptional machinery. We have previously shown genetically that Sugl interacts with the AD of the yeast activator Ga141. Here we provide evidence that the Sugl protein of yeast binds directly to the ADs of Gal4 and the viral activator, VP16. Sugl protein is associated with the TATA-binding protein in vivo and binds to it in vitro, consistent with a mediator function. We also demonstrate that Sugl is not a component of the 26S proteasome, contrary to previous reports2–5. Sugl is a member of a large, highly conserved family of ATPases, implying a role for ATP hydrolysis in the activation of transcription.

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

Similar content being viewed by others

References

  1. Swaffield, J. C., Bromberg, J. & Johnston, S. A. Nature 357, 698–700 (1992).

    Article  ADS  CAS  PubMed  Google Scholar 

  2. Dubiel, W., Ferrell, K., Pratt, G. & Rechsteiner, M. J. biol. Chem. 267, 22699–22702 (1992).

    CAS  PubMed  Google Scholar 

  3. Dubiel, W., Ferrell, K. & Rechsteiner, M. FEBS Lett. 323, 276–278 (1993).

    Article  CAS  PubMed  Google Scholar 

  4. Rechsteiner, M., Hoffman, L. & Dubiel, W. J. biol. Chem. 268, 6065–6068 (1993).

    CAS  PubMed  Google Scholar 

  5. Ghislain, M., Udvardy, A. & Mann, C. Nature 366, 358–362 (1993).

    Article  ADS  CAS  PubMed  Google Scholar 

  6. Berger, S. L. et al. Cell 70, 251–265 (1992).

    Article  CAS  PubMed  Google Scholar 

  7. Nishizawa, M., Suzuki, Y., Nogi, Y., Matsumoto, Y. & Fukasawa, T. Proc. natn. Acad. Sci. U.S.A. 87, 5373–5377 (1990).

    Article  ADS  CAS  Google Scholar 

  8. Himmelfarb, H. J., Pearlberg, J., Last, D. H. & Ptashne, M. Cell 63, 1299–1309 (1990).

    Article  CAS  PubMed  Google Scholar 

  9. Gordon, C., McGurk, G., Dillon, P., Rosen, C. & Hastie, N. D. Nature 366, 355–357 (1993).

    Article  ADS  CAS  PubMed  Google Scholar 

  10. DeMartino, G. et al. J. biol. Chem. 269, 20878–20884 (1994).

    CAS  PubMed  Google Scholar 

  11. McGuire, M. J., McCullough, M. L., Croall, D. E. & DeMartino, G. N. Biochim. biophys. Acta 995, 181–186 (1989).

    Article  CAS  PubMed  Google Scholar 

  12. Eytan, E., Ganoth, D., Armon, T. & Hershko, A. Proc. natn. Acad. Sci. U.S.A. 86, 7751–7755 (1989).

    Article  ADS  CAS  Google Scholar 

  13. Leuther, K. K., Salmeron, J. M. & Johnston, S. A. Cell 72, 575–585 (1993).

    Article  CAS  PubMed  Google Scholar 

  14. Triezenberg, S. J., LaMarco, K. L. & McKnight, S. L. Genes Dev. 2, 730–742 (1988).

    Article  CAS  PubMed  Google Scholar 

  15. Lue, N. F., Chasman, D. I., Buchman, A. R. & Kornberg, R. D. Molec. cell. Biol. 7, 3446–3451 (1987).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  16. Confalonieri, F., Marsault, J. & Duguet, M. J. molec. Biol. 235, 396–401 (1994).

    Article  CAS  PubMed  Google Scholar 

  17. Tomayazu, T. et al. J. Sact. 175, 1344–1351 (1993).

    Google Scholar 

  18. Söllner, T., Bennett, M. K., Whiteheart, S. W., Scheller, R. H. & Rothman, J. E. Cell 75, 409–418 (1993).

    Article  PubMed  Google Scholar 

  19. Erdmann, R. et al. Cell 64, 499–510 (1991).

    Article  CAS  PubMed  Google Scholar 

  20. Thorsness, P. E., White, K. H., Fox, T. D. Molec. cell. Biol. 13, 5418–5426 (1993).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  21. Nobrega, F. G., Nobrega, M. P. & Tzagoloff, A. EMBO J. 11, 3821–3829 (1992).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  22. Kim, Y.-J., Bjorklund, S., Li, Y., Sayre, M. H. & Kornberg, R. D. Cell 77, 599–608 (1994).

    Article  CAS  PubMed  Google Scholar 

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

    Article  ADS  CAS  PubMed  Google Scholar 

  24. O'Connor, V., Augustine, G. J. & Betz, H. Cell 76, 785–787 (1994).

    Article  CAS  PubMed  Google Scholar 

  25. Lee, J. W., Ryan, F., Swaffield, J. C., Johnston, S. A. & Moore, D. D. Nature 374, 91–94 (1995).

    Article  ADS  CAS  PubMed  Google Scholar 

  26. Cormack, B. P., Strubin, M., Ponticelli, A. S. & Struhl, K. Cell 65, 341–348 (1991).

    Article  CAS  PubMed  Google Scholar 

  27. Gill, G. & Tjian, R. Cell 65, 333–340 (1991).

    Article  CAS  PubMed  Google Scholar 

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

    CAS  PubMed  Google Scholar 

  29. Waxman, L., Fagan, J. M. & Goldberg, A. L. J. biol. Chem. 262, 2451–2457 (1987).

    CAS  PubMed  Google Scholar 

  30. Ma, C.-P., Slaughter, C. A. & DeMartino, G. N. J. biol. Chem. 267, 10515–10523 (1992).

    CAS  PubMed  Google Scholar 

Download references

Author information

Author notes

  1. Stephen Albert Johnston: To whom correspondence should be addressed.

Authors and Affiliations

  1. Departments of Medicine and Biochemistry, University of Texas Southwestern Medical Center, Dallas, Texas, 75325-8573, USA

    Jonathan C. Swaffield, Karsten Melcher & Stephen Albert Johnston

Authors
  1. Jonathan C. Swaffield
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Karsten Melcher
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Stephen Albert Johnston
    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

Swaffield, J., Melcher, K. & Johnston, S. A highly conserved ATPase protein as a mediator between acidic activation domains and the TATA-binding protein. Nature 374, 88–91 (1995). https://doi.org/10.1038/374088a0

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1038/374088a0

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

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