Mechanisms for ATP-dependent chromatin remodelling

the means to the end

Andrew Flaus, Tom Owen-Hughes

    Research output: Contribution to journalReview article

    62 Citations (Scopus)

    Abstract

    Chromatin remodelling is the ATP-dependent change in nucleosome organisation driven by Snf2 family ATPases. The biochemistry of this process depends on the behaviours of ATP-dependent motor proteins and their dynamic nucleosome substrates, which brings significant technical and conceptual challenges. Steady progress has been made in characterising the polypeptides of which these enzymes are comprised. Divergence in the sequences of different subfamilies of Snf2-related proteins suggests that the motors are adapted for different functions. Recently, structural insights have suggested that the Snf2 ATPase acts as a context-sensitive DNA translocase. This may have arisen as a means to enable efficient access to DNA in the high density of the eukaryotic nucleus. How the enzymes engage nucleosomes and how the network of noncovalent interactions within the nucleosome respond to the force applied remains unclear, and it remains prudent to recognise the potential for both DNA distortions and dynamics within the underlying histone octamer structure.

    Original languageEnglish
    Pages (from-to)3579-3595
    Number of pages17
    JournalFEBS Journal
    Volume278
    Issue number19
    DOIs
    Publication statusPublished - Oct 2011

    Keywords

    • ATP dependent chromatin remodelling
    • Chd1
    • histone
    • Iswi
    • nucleosome
    • Snf2
    • SWI/SNF
    • YEAST SWI/SNF COMPLEX
    • NUCLEOTIDE EXCISION-REPAIR
    • SACCHAROMYCES-CEREVISIAE
    • RNA-POLYMERASE
    • SNF2 FAMILY
    • IN-VIVO
    • ISW2-NUCLEOSOME COMPLEX
    • NUCLEOSOME MOBILIZATION
    • HISTONE MODIFICATIONS
    • FUNCTIONAL-ANALYSIS

    Cite this

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    title = "Mechanisms for ATP-dependent chromatin remodelling: the means to the end",
    abstract = "Chromatin remodelling is the ATP-dependent change in nucleosome organisation driven by Snf2 family ATPases. The biochemistry of this process depends on the behaviours of ATP-dependent motor proteins and their dynamic nucleosome substrates, which brings significant technical and conceptual challenges. Steady progress has been made in characterising the polypeptides of which these enzymes are comprised. Divergence in the sequences of different subfamilies of Snf2-related proteins suggests that the motors are adapted for different functions. Recently, structural insights have suggested that the Snf2 ATPase acts as a context-sensitive DNA translocase. This may have arisen as a means to enable efficient access to DNA in the high density of the eukaryotic nucleus. How the enzymes engage nucleosomes and how the network of noncovalent interactions within the nucleosome respond to the force applied remains unclear, and it remains prudent to recognise the potential for both DNA distortions and dynamics within the underlying histone octamer structure.",
    keywords = "ATP dependent chromatin remodelling, Chd1, histone, Iswi, nucleosome, Snf2, SWI/SNF, YEAST SWI/SNF COMPLEX, NUCLEOTIDE EXCISION-REPAIR, SACCHAROMYCES-CEREVISIAE, RNA-POLYMERASE, SNF2 FAMILY, IN-VIVO, ISW2-NUCLEOSOME COMPLEX, NUCLEOSOME MOBILIZATION, HISTONE MODIFICATIONS, FUNCTIONAL-ANALYSIS",
    author = "Andrew Flaus and Tom Owen-Hughes",
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    language = "English",
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    Mechanisms for ATP-dependent chromatin remodelling : the means to the end. / Flaus, Andrew; Owen-Hughes, Tom.

    In: FEBS Journal, Vol. 278, No. 19, 10.2011, p. 3579-3595.

    Research output: Contribution to journalReview article

    TY - JOUR

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    T2 - the means to the end

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    AU - Owen-Hughes, Tom

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    N2 - Chromatin remodelling is the ATP-dependent change in nucleosome organisation driven by Snf2 family ATPases. The biochemistry of this process depends on the behaviours of ATP-dependent motor proteins and their dynamic nucleosome substrates, which brings significant technical and conceptual challenges. Steady progress has been made in characterising the polypeptides of which these enzymes are comprised. Divergence in the sequences of different subfamilies of Snf2-related proteins suggests that the motors are adapted for different functions. Recently, structural insights have suggested that the Snf2 ATPase acts as a context-sensitive DNA translocase. This may have arisen as a means to enable efficient access to DNA in the high density of the eukaryotic nucleus. How the enzymes engage nucleosomes and how the network of noncovalent interactions within the nucleosome respond to the force applied remains unclear, and it remains prudent to recognise the potential for both DNA distortions and dynamics within the underlying histone octamer structure.

    AB - Chromatin remodelling is the ATP-dependent change in nucleosome organisation driven by Snf2 family ATPases. The biochemistry of this process depends on the behaviours of ATP-dependent motor proteins and their dynamic nucleosome substrates, which brings significant technical and conceptual challenges. Steady progress has been made in characterising the polypeptides of which these enzymes are comprised. Divergence in the sequences of different subfamilies of Snf2-related proteins suggests that the motors are adapted for different functions. Recently, structural insights have suggested that the Snf2 ATPase acts as a context-sensitive DNA translocase. This may have arisen as a means to enable efficient access to DNA in the high density of the eukaryotic nucleus. How the enzymes engage nucleosomes and how the network of noncovalent interactions within the nucleosome respond to the force applied remains unclear, and it remains prudent to recognise the potential for both DNA distortions and dynamics within the underlying histone octamer structure.

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    KW - NUCLEOTIDE EXCISION-REPAIR

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