期刊
FEBS LETTERS
卷 586, 期 16, 页码 2513-2521出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2012.06.017
关键词
Chromatin remodelling; Histones binding; Nucleosomes; Chromodomain; PHD; ATPase; CHD4; NURD
资金
- Medical Research Council UK [G0700762/1]
- Wellcome Trust core award [090532/Z/09/Z]
- MRC [G0700762] Funding Source: UKRI
- Medical Research Council [G0700762] Funding Source: researchfish
CHD4, the core subunit of the Nucleosome Remodelling and Deacetylase (NuRD) complex, is a chromatin remodelling ATPase that, in addition to a helicase domain, harbors tandem plant homeo finger and chromo domains. By using a panel of domain constructs we dissect their roles and demonstrate that DNA binding, histone binding and ATPase activities are allosterically regulated. Molecular shape reconstruction from small-angle X-ray scattering reveals extensive domain-domain interactions, which provide a structural explanation for the regulation of CHD4 activities by intramolecular domain communication. Our results demonstrate functional interdependency between domains within a chromatin remodeller. (c) 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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