Structural and functional characterization of a cell cycle associated HDAC1/2 complex reveals the structural basis for complex assembly and nucleosome targeting

被引：50

作者：

Itoh, Toshimasa ^{[1
]}

Fairall, Louise ^{[1
]}

Muskett, Frederick W. ^{[1
]}

Milano, Charles P. ^{[1
]}

Watson, Peter J. ^{[1
]}

Arnaudo, Nadia ^{[2
]}

Saleh, Almutasem ^{[1
]}

Millard, Christopher J. ^{[1
]}

El-Mezgueldi, Mohammed ^{[1
]}

Martino, Fabrizio ^{[2
]}

Schwabe, John W. R. ^{[1
]}

机构：

[1] Univ Leicester, Dept Biochem, Henry Wellcome Labs Struct Biol, Leicester LE1 9HN, Leics, England

[2] MRC Lab Mol Biol, Cambridge CB2 0QH, England

来源：

NUCLEIC ACIDS RESEARCH | 2015年 / 43卷 / 04期

基金：

英国惠康基金;

关键词：

PROTEIN; TREP-132; BINDING; DOMAIN; INTERACTS; NURD; SMRT;

D O I：

10.1093/nar/gkv068

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Recent proteomic studies have identified a novel histone deacetylase complex that is upregulated during mitosis and is associated with cyclin A. This complex is conserved from nematodes to man and contains histone deacetylases 1 and 2, the MIDEAS corepressor protein and a protein called DNTTIP1 whose function was hitherto poorly understood. Here, we report the structures of two domains from DNTTIP1. The amino-terminal region forms a tight dimerization domain with a novel structural fold that interacts with and mediates assembly of the HDAC1:MIDEAS complex. The carboxy-terminal domain of DNTTIP1 has a structure related to the SKI/SNO/DAC domain, despite lacking obvious sequence homology. We show that this domain in DNTTIP1 mediates interaction with both DNA and nucleosomes. Thus, DNTTIP1 acts as a dimeric chromatin binding module in the HDAC1: MIDEAS corepressor complex.

引用

页码：2033 / 2044

页数：12

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