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Concerted action of the PHD, chromo and motor domains regulates the human chromatin remodelling ATPase CHD4.

FEBS letters | Jul 30, 2012

http://www.ncbi.nlm.nih.gov/pubmed/22749909

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.

Pubmed ID: 22749909 RIS Download

Mesh terms: Adenosine Triphosphatases | Allosteric Site | Autoantigens | Chromatin | Chromatin Assembly and Disassembly | DNA | DNA Helicases | Escherichia coli | Gene Expression Regulation | Histones | Humans | Kinetics | Mi-2 Nucleosome Remodeling and Deacetylase Complex | Nucleosomes | Protein Binding | Protein Structure, Tertiary | Scattering, Radiation | Surface Plasmon Resonance