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

Rosa Morra; Benjamin M Lee; Heather Shaw; Roman Tuma; Erika J Mancini

doi:10.1016/j.febslet.2012.06.017

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

Rosa Morra
, Benjamin M Lee
, Heather Shaw
, Roman Tuma
, Erika J Mancini

Research output: Contribution to journal › Article › peer-review

Abstract

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.

Original language	English
Pages (from-to)	2513-21
Number of pages	9
Journal	FEBS Letters
Volume	586
Issue number	16
DOIs	https://doi.org/10.1016/j.febslet.2012.06.017
Publication status	Published - 30 Jul 2012

Keywords

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

Research Highlights, Institutes and Platforms

Manchester Cancer Research Centre

Access to Document

10.1016/j.febslet.2012.06.017

Cite this

@article{81a0375e96ed413f948a621d68628eea,

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

abstract = "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.",

keywords = "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",

author = "Rosa Morra and Lee, \{Benjamin M\} and Heather Shaw and Roman Tuma and Mancini, \{Erika J\}",

year = "2012",

month = jul,

day = "30",

doi = "10.1016/j.febslet.2012.06.017",

language = "English",

volume = "586",

pages = "2513--21",

journal = "FEBS Letters",

publisher = "John Wiley \& Sons Ltd",

number = "16",

}

TY - JOUR

T1 - Concerted action of the PHD, chromo and motor domains regulates the human chromatin remodelling ATPase CHD4

AU - Morra, Rosa

AU - Lee, Benjamin M

AU - Shaw, Heather

AU - Tuma, Roman

AU - Mancini, Erika J

PY - 2012/7/30

Y1 - 2012/7/30

N2 - 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.

AB - 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.

KW - Adenosine Triphosphatases

KW - Allosteric Site

KW - Autoantigens

KW - Chromatin

KW - Chromatin Assembly and Disassembly

KW - DNA

KW - DNA Helicases

KW - Escherichia coli

KW - Gene Expression Regulation

KW - Histones

KW - Humans

KW - Kinetics

KW - Mi-2 Nucleosome Remodeling and Deacetylase Complex

KW - Nucleosomes

KW - Protein Binding

KW - Protein Structure, Tertiary

KW - Scattering, Radiation

KW - Surface Plasmon Resonance

U2 - 10.1016/j.febslet.2012.06.017

DO - 10.1016/j.febslet.2012.06.017

M3 - Article

C2 - 22749909

VL - 586

SP - 2513

EP - 2521

JO - FEBS Letters

JF - FEBS Letters

IS - 16

ER -

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

Abstract

Keywords

Research Highlights, Institutes and Platforms

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