Počet záznamů: 1

Physical interaction of RECQ5 helicase with RAD51 facilitates its anti-recombinase activity

  1. 1.
    0347098 - UMG-J 2011 RIV US eng J - Článek v odborném periodiku
    Schwendener, S. - Raynard, S. - Paliwal, S. - Cheng, A. - Kanagaraj, R. - Shevelev, Igor - Stark, J.M. - Sung, P. - Janscak, P.
    Physical interaction of RECQ5 helicase with RAD51 facilitates its anti-recombinase activity.
    Journal of Biological Chemistry. Roč. 285, č. 21 (2010), s. 15739-15745 ISSN 0021-9258
    Grant ostatní: NIH(US) R01CA120954; NIH(US) ES015632; SNSF(CH) 3100A0-116008
    Výzkumný záměr: CEZ:AV0Z50520514
    Klíčová slova: DNA helicase * double-strand breaks * homologous recombination
    Kód oboru RIV: EB - Genetika a molekulární biologie
    Impakt faktor: 5.328, rok: 2010

    Homologous recombination (HR) provides an efficient mechanism for error-free repair of DNA double-strand breaks (DSBs). However, HR can be also harmful as inappropriate or untimely HR events can give rise to lethal recombination intermediates and chromosome rearrangements. A critical step of HR is the formation of a RAD51 filament on single-stranded (ss) DNA, which mediates the invasion of a homologous DNA molecule. In mammalian cells, several DNA helicases have been implicated in the regulation of this process. RECQ5, a member of the RecQ family of DNA helicases, interacts physically with the RAD51 recombinase and disrupts RAD51 presynaptic filaments in a reaction dependent on ATP hydrolysis. Here, we have precisely mapped the RAD51-interacting domain of RECQ5 and generated mutants that fail to interact with RAD51. We show that although these mutants retain normal ATPase activity, they are impaired in their ability to displace RAD51 from ssDNA.
    Trvalý link: http://hdl.handle.net/11104/0187952