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


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


  • Morra R
  • Lee BM
  • Shaw H
  • Tuma R
  • Mancini EJ


FEBS letters

Publication Data

July 30, 2012

Associated Grants

  • Agency: Wellcome Trust, Id: 090532
  • Agency: Wellcome Trust, Id: 90532/Z/09/Z
  • Agency: Medical Research Council, Id: G0700762
  • Agency: Medical Research Council, Id: G0700762/1

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