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    Proc Natl Acad Sci U S A. 2009 Aug 18;106(33):13770-4. Epub 2009 Aug 6.

    Poly(ADP-ribosyl)ation directs recruitment and activation of an ATP-dependent chromatin remodeler.

    Gottschalk AJ, Timinszky G, Kong SE, Jin J, Cai Y, Swanson SK, Washburn MP, Florens L, Ladurner AG, Conaway JW, Conaway RC.

    Source

    The Stowers Institute for Medical Research, 1000 East 50th Street, Kansas City, MO 64110, USA.

    Abstract

    Posttranslational modifications play a key role in recruiting chromatin remodeling and modifying enzymes to specific regions of chromosomes to modulate chromatin structure. Alc1 (amplified in liver cancer 1), a member of the SNF2 ATPase superfamily with a carboxy-terminal macrodomain, is encoded by an oncogene implicated in the pathogenesis of hepatocellular carcinoma. Here we show that Alc1 interacts transiently with chromatin-associated proteins, including histones and the poly(ADP-ribose) polymerase Parp1. Alc1 ATPase and chromatin remodeling activities are strongly activated by Parp1 and its substrate NAD and require an intact macrodomain capable of binding poly(ADP-ribose). Alc1 is rapidly recruited to nucleosomes in vitro and to chromatin in cells when Parp1 catalyzes PAR synthesis. We propose that poly(ADP-ribosyl)ation of chromatin-associated Parp1 serves as a mechanism for targeting a SNF2 family remodeler to chromatin.

    PMID:
    19666485
    [PubMed - indexed for MEDLINE]
    PMCID:
    PMC2722505
    Free PMC Article

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