MRE11 complex links RECQ5 helicase to sites of DNA damage

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68378050%3A_____%2F09%3A00333644" target="_blank" >RIV/68378050:_____/09:00333644 - isvavai.cz</a>
Result on the web
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DOI - Digital Object Identifier
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Result language
angličtina
Original language name
MRE11 complex links RECQ5 helicase to sites of DNA damage
Original language description
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) thatpromotes 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 mediatesbinding 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.
Czech name
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Czech description
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Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
EB - Genetics and molecular biology
OECD FORD branch
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Project
<a href="/en/project/GA204%2F09%2F0565" target="_blank" >GA204/09/0565: Role of RECQ5 DNA helicase in maintenance of genomic stability</a><br>
Continuities
Z - Vyzkumny zamer (s odkazem do CEZ)

Publication year
2009
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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