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PDBsum entry 4ouf
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References listed in PDB file
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Key reference
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Title
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Binding of the histone chaperone asf1 to the cbp bromodomain promotes histone acetylation.
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Authors
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C.Das,
S.Roy,
S.Namjoshi,
C.S.Malarkey,
D.N.Jones,
T.G.Kutateladze,
M.E.Churchill,
J.K.Tyler.
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Ref.
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Proc Natl Acad Sci U S A, 2014,
111,
E1072.
[DOI no: ]
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PubMed id
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Abstract
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The multifunctional Creb-binding protein (CBP) protein plays a pivotal role in
many critical cellular processes. Here we demonstrate that the bromodomain of
CBP binds to histone H3 acetylated on lysine 56 (K56Ac) with higher affinity
than to its other monoacetylated binding partners. We show that autoacetylation
of CBP is critical for the bromodomain-H3 K56Ac interaction, and we propose that
this interaction occurs via autoacetylation-induced conformation changes in CBP.
Unexpectedly, the bromodomain promotes acetylation of H3 K56 on free histones.
The CBP bromodomain also interacts with the histone chaperone anti-silencing
function 1 (ASF1) via a nearby but distinct interface. This interaction is
necessary for ASF1 to promote acetylation of H3 K56 by CBP, indicating that the
ASF1-bromodomain interaction physically delivers the histones to the histone
acetyl transferase domain of CBP. A CBP bromodomain mutation manifested in
Rubinstein-Taybi syndrome has compromised binding to both H3 K56Ac and ASF1,
suggesting that these interactions are important for the normal function of CBP.
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