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FEBS Lett. 2012 Jul 30;586(16):2513-21. doi: 10.1016/j.febslet.2012.06.017. Epub 2012 Jun 27.

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

Author information

1
Division of Structural Biology, Wellcome Trust Centre for Human Genetics, Oxford University, Roosevelt Drive, Oxford OX3 7BN, United Kingdom.

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.

PMID:
22749909
PMCID:
PMC3476528
DOI:
10.1016/j.febslet.2012.06.017
[Indexed for MEDLINE]
Free PMC Article

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