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PDBsum entry 2kwk
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Metal binding protein
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PDB id
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2kwk
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References listed in PDB file
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Key reference
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Title
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Mechanism and regulation of acetylated histone binding by the tandem phd finger of dpf3b.
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Authors
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L.Zeng,
Q.Zhang,
S.Li,
A.N.Plotnikov,
M.J.Walsh,
M.M.Zhou.
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Ref.
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Nature, 2010,
466,
258-262.
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PubMed id
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Abstract
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Histone lysine acetylation and methylation have an important role during gene
transcription in a chromatin context. Knowledge concerning the types of protein
modules that can interact with acetyl-lysine has so far been limited to
bromodomains. Recently, a tandem plant homeodomain (PHD) finger (PHD1-PHD2, or
PHD12) of human DPF3b, which functions in association with the BAF chromatin
remodelling complex to initiate gene transcription during heart and muscle
development, was reported to bind histones H3 and H4 in an acetylation-sensitive
manner, making it the first alternative to bromodomains for acetyl-lysine
binding. Here we report the structural mechanism of acetylated histone binding
by the double PHD fingers of DPF3b. Our three-dimensional solution structures
and biochemical analysis of DPF3b highlight the molecular basis of the
integrated tandem PHD finger, which acts as one functional unit in the
sequence-specific recognition of lysine-14-acetylated histone H3 (H3K14ac).
Whereas the interaction with H3 is promoted by acetylation at lysine 14, it is
inhibited by methylation at lysine 4, and these opposing influences are
important during transcriptional activation of the mouse DPF3b target genes
Pitx2 and Jmjd1c. Binding of this tandem protein module to chromatin can thus be
regulated by different histone modifications during the initiation of gene
transcription.
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