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Binding of the histone chaperone ASF1 to the CBP bromodomain promotes histone acetylation.

Abstract：

: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.

journal_name

Proc Natl Acad Sci U S A

journal_title

Proceedings of the National Academy of Sciences of the United States of America

authors

Das C,Roy S,Namjoshi S,Malarkey CS,Jones DN,Kutateladze TG,Churchill ME,Tyler JK

doi

10.1073/pnas.1319122111

subject

Has Abstract

pub_date

2014-03-25 00:00:00

pages

E1072-81

issue

12

eissn

0027-8424

issn

1091-6490

pii

1319122111

journal_volume

111

pub_type

杂志文章

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