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MRE11 complex links RECQ5 helicase to sites of DNA damage
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SYSNO ASEP 0333644 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název MRE11 complex links RECQ5 helicase to sites of DNA damage Tvůrce(i) Zheng, L. (CH)
Kanagaraj, R. (CH)
Mihaljevic, B. (CH)
Schwendener, S. (CH)
Sartori, A.A. (CH)
Gerrits, B. (CH)
Shevelev, Igor (UMG-J)
Janščák, Pavel (UMG-J) RIDCelkový počet autorů 8 Zdroj.dok. Nucleic Acids Research. - : Oxford University Press - ISSN 0305-1048
Roč. 37, č. 8 (2009), s. 2645-2657Poč.str. 13 s. Jazyk dok. eng - angličtina Země vyd. GB - Velká Británie Klíč. slova homologous recombination, ; RECQ5 helicase ; MRE11 ; DNA repair Vědní obor RIV EB - Genetika a molekulární biologie CEP GA204/09/0565 GA ČR - Grantová agentura ČR CEZ AV0Z50520514 - UMG-J (2005-2011) UT WOS 000265953000029 DOI 10.1093/nar/gkp147 Anotace 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. Pracoviště Ústav molekulární genetiky Kontakt Nikol Škňouřilová, nikol.sknourilova@img.cas.cz, Tel.: 241 063 217 Rok sběru 2010
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