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MRE11 complex links RECQ5 helicase to sites of DNA damage

  1. 1. 0333644 - UMG-J 2010 RIV GB eng J - Journal Article
    Zheng, L. - Kanagaraj, R. - Mihaljevic, B. - Schwendener, S. - Sartori, A.A. - Gerrits, B. - Shevelev, Igor - Janščák, Pavel
    MRE11 complex links RECQ5 helicase to sites of DNA damage.
    Nucleic Acids Research. Roč. 37, č. 8 (2009), s. 2645-2657 ISSN 0305-1048
    R&D Projects: GA ČR GA204/09/0565
    Institutional research plan: CEZ:AV0Z50520514
    Keywords : homologous recombination, * RECQ5 helicase * MRE11 * DNA repair
    Subject RIV: EB - Genetics ; Molecular Biology
    Impact factor: 7.479, year: 2009

    RECQ5 DNA helicase suppresses homologous recombination (HR) possibly through disruption of RAD51 filaments. 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 ATM kinase. Experiments indicated that RECQ5 interacts with the MRN complex through both MRE11 and NBS1, and 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 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. These data suggest that the MRN complex recruits RECQ5 to sites of DNA damage to regulate DNA repair.
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