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

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.

SUBMITTER: Morra R

PROVIDER: S-EPMC3476528 | biostudies-literature | 2012 Jul

REPOSITORIES: biostudies-literature

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

Morra Rosa R Lee Benjamin M BM Shaw Heather H Tuma Roman R Mancini Erika J EJ

FEBS letters 20120627 16

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 ...[more]

PMID: 22749909

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

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