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Physical interaction of RECQ5 helicase with RAD51 facilitates its anti-recombinase activity
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SYSNO ASEP 0347098 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Physical interaction of RECQ5 helicase with RAD51 facilitates its anti-recombinase activity Tvůrce(i) Schwendener, S. (CH)
Raynard, S. (US)
Paliwal, S. (CH)
Cheng, A. (US)
Kanagaraj, R. (CH)
Shevelev, Igor (UMG-J)
Stark, J.M. (US)
Sung, P. (US)
Janscak, P. (CH)Zdroj.dok. Journal of Biological Chemistry. - : Elsevier - ISSN 0021-9258
Roč. 285, č. 21 (2010), s. 15739-15745Poč.str. 6 s. Jazyk dok. eng - angličtina Země vyd. US - Spojené státy americké Klíč. slova DNA helicase ; double-strand breaks ; homologous recombination Vědní obor RIV EB - Genetika a molekulární biologie CEZ AV0Z50520514 - UMG-J (2005-2011) UT WOS 000277715900009 DOI 10.1074/jbc.M110.110478 Anotace 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. Pracoviště Ústav molekulární genetiky Kontakt Nikol Škňouřilová, nikol.sknourilova@img.cas.cz, Tel.: 241 063 217 Rok sběru 2011
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