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    DNA Repair Factor APLF Is a Histone Chaperone.

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    Authors
    Mehrotra, Pawan Vinod
    Ahel, Dragana
    Ryan, D
    Weston, Ria
    Wiechens, N
    Kraehenbuehl, Rolf
    Owen-Hughes, T
    Ahel, Ivan
    Affiliation
    Cancer Research UK, Paterson Institute for Cancer Research, University of Manchester, Wilmslow Road, Manchester M20 4BX, UK.
    Issue Date
    2011-01-07
    
    Metadata
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    Abstract
    Poly(ADP-ribosyl)ation plays a major role in DNA repair, where it regulates chromatin relaxation as one of the critical events in the repair process. However, the molecular mechanism by which poly(ADP-ribose) modulates chromatin remains poorly understood. Here we identify the poly(ADP-ribose)-regulated protein APLF as a DNA-damage-specific histone chaperone. APLF preferentially binds to the histone H3/H4 tetramer via its C-terminal acidic motif, which is homologous to the motif conserved in the histone chaperones of the NAP1L family (NAP1L motif). We further demonstrate that APLF exhibits histone chaperone activities in a manner that is dependent on its acidic domain and that the NAP1L motif is critical for the repair capacity of APLF in vivo. Finally, we identify structural analogs of APLF in lower eukaryotes with the ability to bind histones and localize to the sites of DNA-damage-induced poly(ADP-ribosyl)ation. Collectively, these findings define the involvement of histone chaperones in poly(ADP-ribose)-regulated DNA repair reactions.
    Citation
    DNA Repair Factor APLF Is a Histone Chaperone. 2011, 41 (1):46-55 Mol Cell
    Journal
    Molecular Cell
    URI
    http://hdl.handle.net/10541/120249
    DOI
    10.1016/j.molcel.2010.12.008
    PubMed ID
    21211722
    Type
    Article
    Language
    en
    ISSN
    1097-4164
    ae974a485f413a2113503eed53cd6c53
    10.1016/j.molcel.2010.12.008
    Scopus Count
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    All Paterson Institute for Cancer Research

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