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

Daniel P. Ryan, Ramasubramanian Sundaramoorthy, David Martin, Vijender Singh, Tom Owen-Hughes (Lead / Corresponding author)

    Research output: Contribution to journalArticle

    71 Citations (Scopus)
    103 Downloads (Pure)

    Abstract

    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

    Original languageEnglish
    Pages (from-to)2596-2609
    Number of pages14
    JournalEMBO Journal
    Volume30
    Issue number13
    DOIs
    Publication statusPublished - 6 Jul 2011

    Keywords

    • Chd1
    • DNA binding
    • nucleosomes
    • SANT
    • SLIDE
    • SACCHAROMYCES-CEREVISIAE
    • PROTEIN-STRUCTURE
    • IN-VIVO
    • NUCLEOSOME
    • YEAST
    • ISWI
    • CHROMODOMAINS
    • COMPLEXES
    • ACF
    • TRANSCRIPTION

    Cite this

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    title = "The DNA-binding domain of the Chd1 chromatin-remodelling enzyme contains SANT and SLIDE domains",
    abstract = "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",
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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

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    AU - Sundaramoorthy, Ramasubramanian

    AU - Martin, David

    AU - Singh, Vijender

    AU - Owen-Hughes, Tom

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