Biophysical Characterization of Chromatin Remodeling Protein CHD4

Rosa Morra, Tomas Fessl, Yuchong Wang, Erika J Mancini, Roman Tuma

    Research output: Contribution to journalArticlepeer-review

    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.

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

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