Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 422, Issue 1, Pages 3-17Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2012.04.031
Keywords
NuRD complex; chromatin remodeling; chromo domain helicase DNA-binding protein 4; histone; transcriptional regulation
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Funding
- European Molecular Biology Laboratory interdisciplinary postdoctoral fellowship (EIPOD)
- Abbott
- Canadian Institutes for Health Research
- Canadian Foundation for Innovation
- Eli Lilly and Company
- Genome Canada
- GlaxoSmithKline
- Ontario Ministry of Economic Development and Innovation
- Novartis Research Foundation
- Pfizer
- Wellcome Trust
- MRC [MC_UP_1102/2] Funding Source: UKRI
- Wellcome Trust [095062/Z/10/Z] Funding Source: Wellcome Trust
- Medical Research Council [MC_UP_1102/2] Funding Source: researchfish
- Wellcome Trust [095062/Z/10/Z] Funding Source: researchfish
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The NuRD (nucleosome remodeling and deacetylase) complex serves as a crucial epigenetic regulator of cell differentiation, proliferation, and hematopoietic development by coupling the deacetylation and demethylation of histones, nucleosome mobilization, and the recruitment of transcription factors. The core nucleosome remodeling function of the mammalian NuRD complex is executed by the helicase-domain-containing ATPase CHD4 (Mi-2 beta) subunit, which also contains N-terminal plant homeodomain (PHD) and chromo domains. The mode of regulation of chromatin remodeling by CHD4 is not well understood, nor is the role of its PHD and chromo domains. Here, we use small-angle X-ray scattering, nucleosome binding ATPase and remodeling assays, limited proteolysis, cross-linking, and tandem mass spectrometry to propose a three-dimensional structural model describing the overall shape and domain interactions of CHD4 and discuss the relevance of these for regulating the remodeling of chromatin by the NuRD complex. (C) 2012 Elsevier Ltd. All rights reserved.
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