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Permanent URL to this publication: http://dx.doi.org/10.5167/uzh-34123

Schwendener, S; Raynard, S; Paliwal, S; Cheng, A; Kanagaraj, R; Shevelev, I; Stark, J M; Sung, P; Janscak, P (2010). Physical interaction of RECQ5 helicase with RAD51 facilitates its anti-recombinase activity. Journal of Biological Chemistry, 285(21):15739-15745.

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Abstract

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. Moreover, we show that ablation of RECQ5-RAD51 complex formation by a point mutation alleviates the inhibitory effect of RECQ5 on HR-mediated DSB repair. These findings provide support for the proposal that interaction with RAD51 is critical for the anti-recombinase attribute of RECQ5.

Item Type:Journal Article, refereed, original work
Communities & Collections:04 Faculty of Medicine > Institute of Molecular Cancer Research
07 Faculty of Science > Institute of Molecular Cancer Research
DDC:570 Life sciences; biology
Language:English
Date:21 May 2010
Deposited On:17 May 2010 21:57
Last Modified:27 Nov 2013 19:45
Publisher:American Society for Biochemistry and Molecular Biology
ISSN:0021-9258
Publisher DOI:10.1074/jbc.M110.110478
PubMed ID:20348101
Citations:Web of Science®. Times Cited: 26
Google Scholar™
Scopus®. Citation Count: 32

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