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.

  • Article
  • Published:

Structural similarity between TAFs and the heterotetrameric core of the histone octamer

Abstract

A complex of two TFIID TATA box-binding protein-associated factors (TAFIIs) is described at 2.0 Å resolution. The amino-terminal portions of dTAFII42 and dTAFII62 from Drosophila adopt the canonical histone fold, consisting of two short α-helices flanking a long central α-helix. Like histones H3 and H4, dTAFII42 and dTAFII62 form an intimate heterodimer by extensive hydrophobic contacts between the paired molecules. In solution and in the crystalline state, the dTAFII42/dTAFII62 complex exists as a heterotetramer, resembling the (H3/H4)2 heterotetrameric core of the histone octamer, suggesting that TFIID contains a histone octamer-like substructure.

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. Roeder, R. G. Trends biochem. Sci 16, 402–408 (1991).

    Article  CAS  Google Scholar 

  2. Hori, R. & Carey, M. Curr. Opin. Genet. Dev. 4, 236–244 (1994).

    Article  CAS  Google Scholar 

  3. Zawel, L. & Reinberg, D. Prog. Nucleic Acid Res. molec. Biol. 44, 67–108 (1993).

    Article  CAS  Google Scholar 

  4. Zawel, L., Kumar, K. & Reinberg, D. Genes Dev. 9, 1479–1490 (1995).

    Article  CAS  Google Scholar 

  5. Koleske, A. & Young, R. Trends biochem. Sci. 20, 113–116 (1995).

    Article  CAS  Google Scholar 

  6. Matsui, T., Segall, J., Weil, P. & Roeder, R. G. J. biol. Chem. 255, 11992–11996 (1980).

    CAS  Google Scholar 

  7. Sawadogo, M. & Roeder, R. G. Cell 43, 165–175 (1985).

    Article  CAS  Google Scholar 

  8. Kim, J. L. & Burley, S. K. Nature Struct. Biol. 1, 638–653 (1994).

    Article  CAS  Google Scholar 

  9. Burley, S. K. & Roeder, R. G. A. Rev. Biochem. 65 (in the press).

  10. Owen-Hughes, T. & Workman, J. L. Crit. Rev. Euk. Gene Express. 4, 403–441 (1994).

    CAS  Google Scholar 

  11. Nikolov, D. B. & Burley, S. K. Nature Struct. Biol. 1, 621–637 (1994).

    Article  CAS  Google Scholar 

  12. Reese, J., Apone, L., Walker, S., Griffin, L. & Green, M. Nature 371, 523–527 (1994).

    Article  ADS  CAS  Google Scholar 

  13. Poon, D. et al. Proc. natn. Acad. Sci. U.S.A. 92, 8224–8228 (1995).

    Article  ADS  CAS  Google Scholar 

  14. Chen, J., Attardi, L., Verrijzer, D., Yokomori, K. & Tijan, R. Cell 79, 93–105 (1994).

    Article  CAS  Google Scholar 

  15. Sauer, F., Hansen, S. & Tijan, R. Science 270, 1783–1788 (1995).

    Article  ADS  CAS  Google Scholar 

  16. Kokubo, T. et al. Nature 367, 484–487 (1994).

    Article  ADS  CAS  Google Scholar 

  17. Hisatake, K. et al. Proc. natn. Acad. Sci. U.S.A. 92, 8195–8199 (1995).

    Article  ADS  CAS  Google Scholar 

  18. Hoffmann, A. et al. Nature 380, 356–359 (1996).

    Article  ADS  CAS  Google Scholar 

  19. Baxevanis, A., Arents, G., Moudrianakis, E. & Landsman, D. Nucleic Acids Res. 23, 2685–2691 (1995).

    Article  CAS  Google Scholar 

  20. Goodrich, J., Hoey, T., Thut, C., Admon, A. & Tjian, R. Cell 75, 519–30 (1993).

    Article  CAS  Google Scholar 

  21. Weinzierl, R., Ruppert, S., Dynlacht, B., Tanese, N. & Tjian, R. EMBO J. 12, 5303–5309 (1993).

    Article  CAS  Google Scholar 

  22. Mengus, G. et al. EMBO J. 14, 1520–1531 (1995).

    Article  CAS  Google Scholar 

  23. Yokomori, K., Chen, J.-L., Admon, A., Zhou, S. & Tjian, R. Genes Dev. 7, 2587–2597 (1993).

    Article  CAS  Google Scholar 

  24. Clark, K. L., Halay, E. D., Lai, E. & Burley, S. K. Nature 364, 412–420 (1993).

    Article  ADS  CAS  Google Scholar 

  25. Ramakrishnan, V., Finch, J., Graziano, V. & Sweet, R. Nature 362, 219–223 (1993).

    Article  ADS  CAS  Google Scholar 

  26. McPherson, C., Shin, E.-Y., Friedman, D. & Zaret, K. Cell 75, 387–398 (1993).

    Article  CAS  Google Scholar 

  27. D'Arcy, A. Acta crystallogr. D50, 469–411 (1994).

    CAS  Google Scholar 

  28. Ferré-D'Amaré, A. R. & Burley, S. K. Structure 2, 357–359, 567 (1994).

    Article  Google Scholar 

  29. Cohen, S. L., Ferre-D'Amare, A. R., Burley, S. K. & Chait, B. T. Protein Sci. 4, 1088–1099 (1995).

    Article  CAS  Google Scholar 

  30. Lattman, E., Burlingame, R., Hatch, C. & Moudrianakis, E. N. Science 216, 1016–1018 (1982).

    Article  ADS  CAS  Google Scholar 

  31. Brünger, A. T. X-PLOR, Version 3.1 manual (Yale University, New Haven, CT, 1992).

    Google Scholar 

  32. Laskowski, R. J., Macarthur, M. W., Moss, D. S. & Thornton, J. M. J. appl. Crystallogr. 26, 283–290 (1993).

    Article  CAS  Google Scholar 

  33. Arents, G. & Moudrianakis, E. Proc. natn. Acad. Sci. U.S.A. 92, 11170–11174 (1995).

    Article  ADS  CAS  Google Scholar 

  34. Arents, G., Burlingame, R. W., Wang, B.-C., Love, W. E. & Moudrianakis, E. N. Proc. natn. Acad. Sci. U.S.A. 88, 10148–10152 (1991).

    Article  ADS  CAS  Google Scholar 

  35. Karantza, V., Friere, E. & Moudrianakis, E. N. Biochemistry 35 (in the press).

  36. Janin, J. Proteins 21, 30–39 (1995).

    Article  CAS  Google Scholar 

  37. Nikolov, D. B. et al. Nature 377, 119–128 (1995).

    Article  ADS  CAS  Google Scholar 

  38. Klemm, R., Goodrich, J., Zhou, S. & Tjian, R. Proc. natn. Acad. Sci. U.S.A. 92, 92, 5788–5792 (1995).

    Article  ADS  CAS  Google Scholar 

  39. Thut, C., Chen, J. L., Klemm, R. & Tjian, R. Science 267, 100–104 (1995).

    Article  ADS  CAS  Google Scholar 

  40. Lu, H. & Levine, A. Proc. natn. Acad. Sci. U.S.A. 92, 5154–5158 (1995).

    Article  ADS  CAS  Google Scholar 

  41. Horikoshi, M., Carey, M., Kadidani, H. & Roeder, R. G. Cell 54, 665–669 (1988).

    Article  CAS  Google Scholar 

  42. Horikoshi, M., Hai, T., Lin, Y.-S., Green, M. R. & Roeder, R. G. Cell 54, 1033–1042 (1988).

    Article  CAS  Google Scholar 

  43. Lieberman, P. & Berk, A. Genes Dev. 8, 995–1006 (1994).

    Article  CAS  Google Scholar 

  44. Chi, T., Lieberman, P., Ellwood, K. & Carey, M. Nature 377, 254–257 (1995).

    Article  ADS  CAS  Google Scholar 

  45. Tjian, R. & Maniatis, T. Cell 77, 5–8 (1994).

    Article  CAS  Google Scholar 

  46. Klug, A., Rhodes, D., Smith, J., Finch, J. & Thomas, J. Nature 287, 509–516 (1980).

    Article  ADS  CAS  Google Scholar 

  47. Richmond, T., Finch, J., Rushton, B., Rhodes, D. & Klug, A. Nature 311, 532–537 (1984).

    Article  ADS  CAS  Google Scholar 

  48. Arents, G. & Moudrianakis, E. N. Proc. natn. Acad. Sci. U.S.A. 90, 10489–10493 (1993).

    Article  ADS  CAS  Google Scholar 

  49. Pruss, D., Hayes, J. & Wolffe, A. BioEssays 17, 161–170 (1995).

    Article  CAS  Google Scholar 

  50. Hendrickson, W. A. Science 254, 51–58 (1991).

    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

Xie, X., Kokubo, T., Cohen, S. et al. Structural similarity between TAFs and the heterotetrameric core of the histone octamer. Nature 380, 316–322 (1996). https://doi.org/10.1038/380316a0

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1038/380316a0

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