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

0347098 - ÚMG 2011 RIV US eng J - Journal Article
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. E-ISSN 1083-351X
Grant - others:NIH(US) R01CA120954; NIH(US) ES015632; SNSF(CH) 3100A0-116008
Institutional research plan: CEZ:AV0Z50520514
Keywords : DNA helicase * double-strand breaks * homologous recombination
Subject RIV: EB - Genetics ; Molecular Biology
Impact factor: 5.328, year: 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.
Permanent Link: http://hdl.handle.net/11104/0187952