The PHD and Chromo Domains Regulate the ATPase Activity of the Human Chromatin Remodeler CHD4
Copyright policy )The PHD and Chromo Domains Regulate the ATPase Activity of the Human Chromatin Remodeler CHD4
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.
- Wellcome Trust United Kingdom
- University of North Carolina at Chapel Hill United States
- University of Cambridge - Department of Biochemistry United Kingdom
- University of Cambridge United Kingdom
- Cancer Research UK United Kingdom
570, Autoantigens: chemistry, CHD4 protein, human, Electrophoretic Mobility Shift Assay, histone, NuRD complex, Autoantigens: metabolism, Autoantigens, Models, Biological, Article, chromatin remodeling, Humans, transcriptional regulation, Adenosine Triphosphatases: metabolism, Molecular Biology, info:eu-repo/classification/ddc/570, Mi-2 Nucleosome Remodeling and Deacetylase Complex: chemistry, Adenosine Triphosphatases, Binding Sites, chromo domain helicase DNA-binding protein 4, Chromatin: metabolism, 540, Nucleosomes: metabolism, Chromatin Assembly and Disassembly, Chromatin, Nucleosomes, Protein Structure, Tertiary, Proteolysis, Mi-2 Nucleosome Remodeling and Deacetylase Complex: metabolism, Mi-2 Nucleosome Remodeling and Deacetylase Complex
570, Autoantigens: chemistry, CHD4 protein, human, Electrophoretic Mobility Shift Assay, histone, NuRD complex, Autoantigens: metabolism, Autoantigens, Models, Biological, Article, chromatin remodeling, Humans, transcriptional regulation, Adenosine Triphosphatases: metabolism, Molecular Biology, info:eu-repo/classification/ddc/570, Mi-2 Nucleosome Remodeling and Deacetylase Complex: chemistry, Adenosine Triphosphatases, Binding Sites, chromo domain helicase DNA-binding protein 4, Chromatin: metabolism, 540, Nucleosomes: metabolism, Chromatin Assembly and Disassembly, Chromatin, Nucleosomes, Protein Structure, Tertiary, Proteolysis, Mi-2 Nucleosome Remodeling and Deacetylase Complex: metabolism, Mi-2 Nucleosome Remodeling and Deacetylase Complex
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