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Concerted action of the PHD, chromo and motor domains regulates the human chromatin remodelling ATPase CHD4
Author(s) -
Morra Rosa,
Lee Benjamin M.,
Shaw Heather,
Tuma Roman,
Mancini Erika J.
Publication year - 2012
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2012.06.017
Subject(s) - chromatin , microbiology and biotechnology , nucleosome , chromatin remodeling , aaa proteins , helicase , chromatin structure remodeling (rsc) complex , atpase , biology , histone , protein subunit , chemistry , biophysics , dna , biochemistry , enzyme , gene , rna
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.