Structure and Function of a Human TAF II 250 Double Bromodomain Module

American Association for the Advancement of Science (AAAS) - Tập 288 Số 5470 - Trang 1422-1425 - 2000
Raymond H. Jacobson1, Andreas G. Ladurner1, David S. King1, Robert Tjian1
1Howard Hughes Medical Institute and Department of Molecular and Cell Biology, 401 Barker Hall, University of California, Berkeley, CA 94720–3204, USA.

Tóm tắt

TFIID is a large multiprotein complex that initiates assembly of the transcription machinery. It is unclear how TFIID recognizes promoters in vivo when templates are nucleosome-bound. Here, it is shown that TAF II 250, the largest subunit of TFIID, contains two tandem bromodomain modules that bind selectively to multiply acetylated histone H4 peptides. The 2.1 angstrom crystal structure of the double bromodomain reveals two side-by-side, four-helix bundles with a highly polarized surface charge distribution. Each bundle contains an N ɛ -acetyllysine binding pocket at its center, which results in a structure ideally suited for recognition of diacetylated histone H4 tails. Thus, TFIID may be targeted to specific chromatin-bound promoters and may play a role in chromatin recognition.

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Supported in part by grants from the National Institutes of Health The Wellcome Trust and the Burroughs Wellcome Fund. We thank J. Endrizzi for assistance maintaining our diffraction facilities and offering helpful advice. We thank J. Holton for the use of ELVES T. Alber and J. Berger for their insights and observations and T. Earnest and the staff at the Advanced Light Source for their help. We thank T. Handel and her lab for their support D. Koshland Jr. and S. Marqusee for use of the MCS-ITC instrument and M. Haggart for DNA sequencing and oligonucleotide synthesis. We thank D. Rio M. Botchan and B. W. Matthews for their comments on the manuscript.

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American Association for the Advancement of Science (AAAS)

Tập 288 Số 5470

1422-1425

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