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The PHD and chromo domains regulate the ATPase activity of the human chromatin remodeler CHD4

By A. A. Watson, P. Mahajan, H. D. Mertens, M. J. Deery, W. Zhang, P. Pham, X. Du, T. Bartke, C. Edlich, G. Berridge, Y. Chen, N. A. Burgess-Brown, T. Kouzarides, N. Wiechens, T. Owen-Hughes, D. I. Svergun, O. Gileadi and E. D. Laue

Abstract

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-2β) 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

Topics: info:eu-repo/classification/ddc/570, Adenosine Triphosphatases: metabolism, Autoantigens: chemistry, Autoantigens: metabolism, Binding Sites, Chromatin: metabolism, Chromatin Assembly and Disassembly, Electrophoretic Mobility Shift Assay, Humans, Mi-2 Nucleosome Remodeling and Deacetylase Complex: chemistry, Mi-2 Nucleosome Remodeling and Deacetylase Complex: metabolism, Models, Biological, Nucleosomes: metabolism, Protein Structure, Tertiary, Proteolysis, Autoantigens, CHD4 protein, human, Chromatin, Nucleosomes, Mi-2 Nucleosome Remodeling and Deacetylase Complex, Adenosine Triphosphatases
Publisher: Elsevier
Year: 2012
DOI identifier: 10.1016/j.jmb.2012.04.031
OAI identifier: oai:bib-pubdb1.desy.de:140870
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