Abstract
The X-ray crystal structure of the transcription factor IIA (TFIIA)in complex with the TATA-box-binding protein (TBP) and TATA-element DNA is presented at 2.5 Å resolution. TFIIA is composed of a β-barrel and a four-helix bundle motif that together have a boot-like appearance. The β-barrel extends the TBP β-sheet and bridges over the DNA major groove immediately upstream of the TATA box. The four-helix bundle contributes substantially to the surface of the complex available for interaction with additional transcription factors.
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References
Maldonado, E. & Reinberg, D. Curr. Opin. Cell Biol. 7, 352–361 (1995).
Hori, R. & Carey, M. Curr. Opin. Genet. Dev. 4, 236–244 (1994).
Conaway, R. C. & Conaway, J. W. A. Rev. Biochem. 62, 161–190 (1993).
Matsui, T., Segall, J., Weil, P. A. & Roeder, R. G. J. biol. Chem. 255, 11992–11996 (1980).
Reinberg, D., Horikoshi, M. & Roeder, R. G. J. biol. Chem. 262, 3322–3330 (1987).
Sayre, M. H., Tschochner, H. & Kornberg, R. D. J. biol. Chem. 267, 23376–23382 (1992).
Cortes, P., Flores, O. & Reinberg, D. Molec. cell. Biol. 12, 413–421 (1992).
Sun, X., Ma, D., Sheldon, M., Yeung, K. & Reinberg, D. Genes Dev. 8, 2336–2348 (1994).
Hansen, S. K. & Tjian, R. Cell 82, 565–575 (1995).
Imbalzano, A. N., Zaret, K. S. & Kingston, R. E. J. biol. Chem. 269, 8280–8286 (1994).
Ranish, J. A. & Hahn, S. J. biol. Chem. 266, 19320–19327 (1991).
Coulombe, B., Li, J. & Greenblatt, J. J. biol. Chem. 269, 19962–19967 (1994).
De Jong, J., Bernstein, R. & Roeder, R. G. Proc. natn. Acad. Sci. U.S.A. 92, 3313–3317 (1995).
Ozer, J. et al. Genes Dev. 8, 2324–2335 (1994).
Yokomori, K. et al. Genes Dev. 8, 2313–2323 (1994).
Inostroza, J. A., Mermelstein, F. H., Ha, I., Lane, W. S. & Reinberg, D. Cell 70, 477–489 (1992).
Auble, D. T. & Hahn, S. Genes Dev. 7, 844–856 (1993).
Wang, W., Gralla, J. D. & Carey, M. Genes Dev. 6, 1716–1727 (1992).
Ge, H. & Roeder, R. G. Cell 78, 513–523 (1994).
Shykind, B. M., Kim, J. & Sharp, P. A. Genes Dev. 9, 1354–1365 (1995).
Ranish, J. A., Lane, W. S. & Hahn, S. Science 255, 1127–1129 (1992).
Stargell, L. A. & Struhl, K. Science 269, 75–78 (1995).
Zeidler, M. P., Yokomori, K., Tjian, R. & Mlodzik, M. Genes Dev. 10, 50–59 (1996).
De Jong, J. & Roeder, R. G. Genes Dev. 7, 2220–2234 (1993).
Ma, D. et al. Genes Dev. 7, 2246–2257 (1993).
Yokomori, K., Admon, A., Goodrich, J. A., Chen, J. L. & Tjian, R. Genes Dev. 7, 2235–2245 (1993).
Kang, J. J., Auble, D. T., Ranish, J. A. & Hahn, S. Molec. cell. Biol. 15, 1234–1243 (1995).
Nikolov, D. B. et al. Nature 360, 40–46 (1992).
Chasman, D. I., Flaherty, K. M., Sharp, P. A. & Kornberg, R. D. Proc. natn. Acad. Sci. U.S.A. 90, 8174–8178 (1993).
Kim, Y., Geiger, J. H., Hahn, S. & Sigler, P. B. Nature 365, 512–520 (1993).
Kim, J. L., Nikolov, D. B. & Burley, S. K. Nature 365, 520–527 (1993).
Nikolov, D. B. et al. Nature 377, 119–128 (1995).
Buratowski, S. & Zhou, H. Science 255, 1130–1132 (1992).
Lee, D. K., DeJong, J., Hashimoto, S., Horikoshi, M. & Roeder, R. G. Molec. cell. Biol. 12, 5189–5196 (1992).
Tang, H., Sun, X., Reinberg, D. & Ebright, R. H. Proc. natn. Acad. Sci. U.S.A. 93, 1119–1124 (1996).
Breathnach, R. & Chambon, P. A. Rev. Biochem. 50, 349–383 (1981).
Hahn, S., Buratowski, S., Sharp, P. A. & Guarente, L. EMBO J. 8, 3379–3382 (1989).
Buratowski, S., Hahn, S., Guarente, L. & Sharp, P. A. Cell 56, 549–561 (1989).
Studier, F. W., Rosenberg, A. H., Dunn, J. J. & Dubendorff, J. W. Meth. Enzym. 185, 60–89 (1990).
Parks, T. D., Leuther, K. K., Howard, E. D., Johnston, S. A. & Dougherty, W. G. Analyt. Biochem. 216, 413–417 (1994).
Otwinowsky, Z. in Isomorphous Replacement and Anomalous Scattering (eds Wolf, W., Evans, P. R. & Leslie, A. G. W.) 80–86 (SERC, Daresbury Laboratory, Warrington, UK, 1991).
Jones, T. A., Zou, J. Y., Cowan, S. W. & Kjeldgaard, M. Acta crystallogr. A47, 110–119 (1991).
Read, R. J. Acta crystallogr. A42, 140–149 (1986).
Brünger, A. X-PLOR Version 3.1 (Yale University, New Haven, CT, 1992).
Tronrud, D. E. Acta crystallogr. A48, 912–916 (1992).
Lavery, R. & Sklenar, H. J. biomol. Struct. Dynam. 6, 63–91 (1988).
Kabsch, W. & Sander, C. Biopolymers 22, 2577–2637 (1983).
Ferrin, T. E., Huang, C. C., Jarvis, L. E. & Langridge, R. J. molec. Graph. 6, 13–27 (1988).
Nicholls, A., Sharp, K. & Honig, B. Proteins 11, 281–296 (1991).
Li, W. & Sherman, F. Molec. cell. Biol. 11, 666–676 (1991).
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Tan, S., Hunziker, Y., Sargent, D. et al. Crystal structure of a yeast TFIIA/TBP/DNA complex. Nature 381, 127–134 (1996). https://doi.org/10.1038/381127a0
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DOI: https://doi.org/10.1038/381127a0
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