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 TAFII250, 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 Nepsilon-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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Acetylation
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Amino Acid Motifs
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Amino Acid Sequence
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Binding Sites
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Cloning, Molecular
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Crystallography, X-Ray
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DNA-Binding Proteins / chemistry*
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DNA-Binding Proteins / genetics
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DNA-Binding Proteins / metabolism*
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Histone Acetyltransferases
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Histones / metabolism
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Humans
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Lysine / analogs & derivatives
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Lysine / chemistry
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Lysine / metabolism
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Models, Molecular
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Molecular Sequence Data
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Nuclear Proteins / chemistry*
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Nuclear Proteins / genetics
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Nuclear Proteins / metabolism*
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Nucleosomes / metabolism
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Promoter Regions, Genetic
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Protein Binding
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Protein Conformation
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Protein Structure, Secondary
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Protein Structure, Tertiary
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Recombinant Proteins / chemistry
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Recombinant Proteins / metabolism
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TATA-Binding Protein Associated Factors*
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Transcription Factor TFIID*
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Transcription, Genetic*
Substances
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DNA-Binding Proteins
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Histones
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Nuclear Proteins
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Nucleosomes
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Recombinant Proteins
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TATA-Binding Protein Associated Factors
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Transcription Factor TFIID
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N-epsilon-acetyllysine
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Histone Acetyltransferases
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TATA-binding protein associated factor 250 kDa
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Lysine