Biophysical Characterization of Chromatin Remodeling Protein CHD4

Research output: Contribution to journalArticle

  • Authors:
  • Rosa Morra
  • Tomas Fessl
  • Yuchong Wang
  • Erika J Mancini
  • Roman Tuma

Abstract

Chromatin-remodeling ATPases modulate histones-DNA interactions within nucleosomes and regulate transcription. At the heart of remodeling, ATPase is a helicase-like motor flanked by a variety of conserved targeting domains. CHD4 is the core subunit of the nucleosome remodeling and deacetylase complex NuRD and harbors tandem plant homeo finger (tPHD) and chromo (tCHD) domains. We describe a multifaceted approach to link the domain structure with function, using quantitative assays for DNA and histone binding, ATPase activity, shape reconstruction from solution scattering data, and single molecule translocation assays. These approaches are complementary to high-resolution structure determination.

Bibliographical metadata

Original languageEnglish
Pages (from-to)175-93
Number of pages19
JournalMethods in molecular biology (Clifton, N.J.)
Volume1431
DOIs
StatePublished - 10 Jun 2016