MRE11 complex links RECQ5 helicase to sites of DNA damage

Kód výsledku v 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>

Výsledek na webu

—

DOI - Digital Object Identifier

—

Jazyk výsledku

angličtina

Název v původním jazyce

MRE11 complex links RECQ5 helicase to sites of DNA damage

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

MRE11 complex links RECQ5 helicase to sites of DNA damage

Popis výsledku anglicky

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.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

EB - Genetika a molekulární biologie

OECD FORD obor

—

Projekt

<a href="/cs/project/GA204%2F09%2F0565" target="_blank" >GA204/09/0565: Úloha RECQ5 DNA helikázy při udržování stability genomu</a><br>

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2009

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Nucleic Acids Research

ISSN

0305-1048

e-ISSN

—

Svazek periodika

37

Číslo periodika v rámci svazku

8

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

13

Strana od-do

—

Kód UT WoS článku

000265953000029

EID výsledku v databázi Scopus

—