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

Aleksandra A Watson1, Pravin Mahajan, Haydyn D T Mertens

  • 1Department of Biochemistry, University of Cambridge, Cambridge CB2 1GA, UK.

Journal of Molecular Biology
|May 12, 2012
PubMed

Insights

The nucleosome remodeling and deacetylase (NuRD) complex

Area of Science:

  • Epigenetics
  • Molecular Biology
  • Structural Biology

Background:

  • The NuRD complex is a key epigenetic regulator involved in cell differentiation, proliferation, and development.
  • The CHD4 (Mi-2β) subunit is central to the NuRD complex's chromatin remodeling activity.
  • The regulatory mechanisms of CHD4 and its domains (PHD, chromo) remain unclear.

Purpose of the Study:

  • To elucidate the structural basis of chromatin remodeling by the CHD4 subunit.
  • To understand the role of CHD4's PHD and chromo domains in its function.

Main Methods:

  • Small-angle X-ray scattering (SAXS)
  • Nucleosome binding, ATPase, and remodeling assays
  • Limited proteolysis, cross-linking, and tandem mass spectrometry

Main Results:

  • A three-dimensional structural model of CHD4 was proposed.
  • The model describes the overall shape and domain interactions of CHD4.
  • Insights into how CHD4 domains regulate chromatin remodeling were gained.

Conclusions:

  • The study provides a structural framework for understanding CHD4-mediated chromatin remodeling.
  • This work clarifies the role of specific CHD4 domains in NuRD complex function.
  • Findings are relevant for epigenetic regulation and cellular processes controlled by NuRD.

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