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Permanent URL to this publication: http://dx.doi.org/10.5167/uzh-17926

Zheng, L; Kanagaraj, R; Mihaljevic, B; Schwendener, S; Sartori, A A; Gerrits, B; Shevelev, I; Janscak, P (2009). MRE11 complex links RECQ5 helicase to sites of DNA damage. Nucleic Acids Research, 37(8):2645-2657.

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RECQ5 DNA helicase suppresses homologous recombination (HR) possibly through disruption of RAD51 filaments. Here, we show that RECQ5 is constitutively associated with the MRE11-RAD50-NBS1 (MRN) complex, a primary sensor of DNA double-strand breaks (DSBs) that promotes DSB repair and regulates DNA damage signaling via activation of the ATM kinase. Experiments with purified proteins indicated that RECQ5 interacts with the MRN complex through both MRE11 and NBS1. Functional assays revealed that RECQ5 specifically inhibited the 3'-->5' exonuclease activity of MRE11, while MRN had no effect on the helicase activity of RECQ5. At the cellular level, we observed that the MRN complex was required for the recruitment of RECQ5 to sites of DNA damage. Accumulation of RECQ5 at DSBs was neither dependent on MDC1 that mediates binding of MRN to DSB-flanking chromatin nor on CtIP that acts in conjunction with MRN to promote resection of DSBs for repair by HR. Collectively, these data suggest that the MRN complex recruits RECQ5 to sites of DNA damage to regulate DNA repair.


22 citations in Web of Science®
23 citations in Scopus®
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146 downloads since deposited on 25 Mar 2009
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Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:04 Faculty of Medicine > Functional Genomics Center Zurich
04 Faculty of Medicine > Institute of Molecular Cancer Research
07 Faculty of Science > Institute of Molecular Cancer Research

08 University Research Priority Programs > Systems Biology / Functional Genomics
Dewey Decimal Classification:570 Life sciences; biology
610 Medicine & health
Date:May 2009
Deposited On:25 Mar 2009 15:31
Last Modified:05 Apr 2016 13:11
Publisher:Oxford University Press
Additional Information:Full final text Oxford Journal
Publisher DOI:10.1093/nar/gkp147
PubMed ID:19270065

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