The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Structure and Function of a Human TAF II 250 Double Bromodomain Module
Abstract
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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Cites
Structure and ligand of a histone acetyltransferase bromodomain
Dhalluin, C., Carlson, J. E., Zeng, L., He, C., Aggarwal, A. K., Zhou, M.-M., & Zhou, M.-M. (1999) · Nature · doi:10.1038/20974 · Cited by 1,732
Transcription-linked acetylation by Gcn5p of histones H3 and H4 at specific lysines
Kuo, M.-H., Brownell, J. E., Sobel, R. E., Ranalli, T. A., Cook, R. G., Edmondson, D. G., Roth, S. Y., & Allis, C. D. (1996) · Nature · doi:10.1038/383269a0 · Cited by 596
Cited by
Jenuwein, T., & Allis, C. D. (2001) · Science · doi:10.1126/science.1063127 · Cited by 9,756
Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain
Bannister, A. J., Zegerman, P., Partridge, J. F., Miska, E. A., Thomas, J. O., Allshire, R. C., & Kouzarides, T. (2001) · Nature · doi:10.1038/35065138 · Cited by 2,903
Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins
Lachner, M., O'Carroll, D., Rea, S., Mechtler, K., & Jenuwein, T. (2001) · Nature · doi:10.1038/35065132 · Cited by 2,868
Role of Histone H3 Lysine 9 Methylation in Epigenetic Control of Heterochromatin Assembly
Nakayama, J.-I., Rice, J. C., Strahl, B. D., Allis, C. D., & Grewal, S. I. S. (2001) · Science · doi:10.1126/science.1060118 · Cited by 1,739
Functions of Site-Specific Histone Acetylation and Deacetylation
Shahbazian, M. D., & Grunstein, M. (2007) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.76.052705.162114 · Cited by 1,635
Metadata
- Authors
- Jacobson, R. H., Ladurner, A. G., King, D. S., & Tjian, R.
- Venue
- Science
- Published
- 2000-05-26
- Volume
- 288
- Issue
- 5470
- Pages
- 1422-1425
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2085299836
- Cited by
- 843
- References
- 2
- FWCI
- 20.62
- Type
- journal article
- Language
- en
- Open access
- closed
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- Jacobson, R. H., Ladurner, A. G., King, D. S., & Tjian, R. (2000). Structure and Function of a Human TAF II 250 Double Bromodomain Module. Science. https://doi.org/10.1126/science.288.5470.1422
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