Biophysical Characterization of Chromatin Remodeling Protein CHD4

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

doi:10.1007/978-1-4939-3631-1_14

Biophysical Characterization of Chromatin Remodeling Protein CHD4

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

Research output: Contribution to journal › Article › peer-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 language	English
Pages (from-to)	175-93
Number of pages	19
Journal	Methods in molecular biology (Clifton, N.J.)
Volume	1431
DOIs	https://doi.org/10.1007/978-1-4939-3631-1_14
Publication status	Published - 10 Jun 2016

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title = "Biophysical Characterization of Chromatin Remodeling Protein CHD4",

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.",

author = "Rosa Morra and Tomas Fessl and Yuchong Wang and Mancini, {Erika J} and Roman Tuma",

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T1 - Biophysical Characterization of Chromatin Remodeling Protein CHD4

AU - Morra, Rosa

AU - Fessl, Tomas

AU - Wang, Yuchong

AU - Mancini, Erika J

AU - Tuma, Roman

PY - 2016/6/10

Y1 - 2016/6/10

N2 - 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.

AB - 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.

U2 - 10.1007/978-1-4939-3631-1_14

DO - 10.1007/978-1-4939-3631-1_14

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VL - 1431

SP - 175

EP - 193

JO - Methods in Molecular Biology

JF - Methods in Molecular Biology

SN - 1064-3745

ER -

Biophysical Characterization of Chromatin Remodeling Protein CHD4

Abstract

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