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The DNA-binding domain of the Chd1 chromatin-remodelling enzyme contains SANT and SLIDE domains

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The DNA-binding domain of the Chd1 chromatin-remodelling enzyme contains SANT and SLIDE domains. / Ryan, Daniel P.; Sundaramoorthy, Ramasubramanian; Martin, David; Singh, Vijender; Owen-Hughes, Tom (Lead / Corresponding author).

In: EMBO Journal, Vol. 30, No. 13, 06.07.2011, p. 2596-2609.

Research output: Contribution to journalArticle

Harvard

Ryan, DP, Sundaramoorthy, R, Martin, D, Singh, V & Owen-Hughes, T 2011, 'The DNA-binding domain of the Chd1 chromatin-remodelling enzyme contains SANT and SLIDE domains' EMBO Journal, vol 30, no. 13, pp. 2596-2609.

APA

Ryan, D. P., Sundaramoorthy, R., Martin, D., Singh, V., & Owen-Hughes, T. (2011). The DNA-binding domain of the Chd1 chromatin-remodelling enzyme contains SANT and SLIDE domains. EMBO Journal, 30(13), 2596-2609doi: 10.1038/emboj.2011.166

Vancouver

Ryan DP, Sundaramoorthy R, Martin D, Singh V, Owen-Hughes T. The DNA-binding domain of the Chd1 chromatin-remodelling enzyme contains SANT and SLIDE domains. EMBO Journal. 2011 Jul 6;30(13):2596-2609.

Author

Ryan, Daniel P.; Sundaramoorthy, Ramasubramanian; Martin, David; Singh, Vijender; Owen-Hughes, Tom (Lead / Corresponding author) / The DNA-binding domain of the Chd1 chromatin-remodelling enzyme contains SANT and SLIDE domains.

In: EMBO Journal, Vol. 30, No. 13, 06.07.2011, p. 2596-2609.

Research output: Contribution to journalArticle

Bibtex - Download

@article{b03fb55562e44a7c8a623d247c0eace3,
title = "The DNA-binding domain of the Chd1 chromatin-remodelling enzyme contains SANT and SLIDE domains",
author = "Ryan, {Daniel P.} and Ramasubramanian Sundaramoorthy and David Martin and Vijender Singh and Tom Owen-Hughes",
year = "2011",
volume = "30",
number = "13",
pages = "2596--2609",
journal = "EMBO Journal",
issn = "0261-4189",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - The DNA-binding domain of the Chd1 chromatin-remodelling enzyme contains SANT and SLIDE domains

A1 - Ryan,Daniel P.

A1 - Sundaramoorthy,Ramasubramanian

A1 - Martin,David

A1 - Singh,Vijender

A1 - Owen-Hughes,Tom

AU - Ryan,Daniel P.

AU - Sundaramoorthy,Ramasubramanian

AU - Martin,David

AU - Singh,Vijender

AU - Owen-Hughes,Tom

PY - 2011/7/6

Y1 - 2011/7/6

N2 - <p>The ATP-dependent chromatin-remodelling enzyme Chd1 is a 168-kDa protein consisting of a double chromodomain, Snf2-related ATPase domain, and a C-terminal DNA-binding domain. Here, we show the DNA-binding domain is required for Saccharomyces cerevisiae Chd1 to bind and remodel nucleosomes. The crystal structure of this domain reveals the presence of structural homology to SANT and SLIDE domains previously identified in ISWI remodelling enzymes. The presence of these domains in ISWI and Chd1 chromatin-remodelling enzymes may provide a means of efficiently harnessing the action of the Snf2-related ATPase domain for the purpose of nucleosome spacing and provide an explanation for partial redundancy between these proteins. Site directed mutagenesis was used to identify residues important for DNA binding and generate a model describing the interaction of this domain with DNA. Through inclusion of Chd1 sequences in homology searches SLIDE domains were identified in CHD6-9 proteins. Point mutations to conserved amino acids within the human CHD7 SLIDE domain have been identified in patients with CHARGE syndrome. The EMBO Journal (2011) 30, 2596-2609. doi:10.1038/emboj.2011.166; Published online 27 May 2011</p>

AB - <p>The ATP-dependent chromatin-remodelling enzyme Chd1 is a 168-kDa protein consisting of a double chromodomain, Snf2-related ATPase domain, and a C-terminal DNA-binding domain. Here, we show the DNA-binding domain is required for Saccharomyces cerevisiae Chd1 to bind and remodel nucleosomes. The crystal structure of this domain reveals the presence of structural homology to SANT and SLIDE domains previously identified in ISWI remodelling enzymes. The presence of these domains in ISWI and Chd1 chromatin-remodelling enzymes may provide a means of efficiently harnessing the action of the Snf2-related ATPase domain for the purpose of nucleosome spacing and provide an explanation for partial redundancy between these proteins. Site directed mutagenesis was used to identify residues important for DNA binding and generate a model describing the interaction of this domain with DNA. Through inclusion of Chd1 sequences in homology searches SLIDE domains were identified in CHD6-9 proteins. Point mutations to conserved amino acids within the human CHD7 SLIDE domain have been identified in patients with CHARGE syndrome. The EMBO Journal (2011) 30, 2596-2609. doi:10.1038/emboj.2011.166; Published online 27 May 2011</p>

KW - Chd1

KW - DNA binding

KW - nucleosomes

KW - SANT

KW - SLIDE

KW - SACCHAROMYCES-CEREVISIAE

KW - PROTEIN-STRUCTURE

KW - IN-VIVO

KW - NUCLEOSOME

KW - YEAST

KW - ISWI

KW - CHROMODOMAINS

KW - COMPLEXES

KW - ACF

KW - TRANSCRIPTION

UR - http://ukpmc.ac.uk/articles/PMC3155300

U2 - 10.1038/emboj.2011.166

DO - 10.1038/emboj.2011.166

M1 - Article

JO - EMBO Journal

JF - EMBO Journal

SN - 0261-4189

IS - 13

VL - 30

SP - 2596

EP - 2609

ER -

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