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

Authors:
Morra R, Lee BM, Shaw H, Tuma R, Mancini EJ
Affiliation:
Journal:
FEBS letters

Abstract

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.

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