2017
Role of PCNA and RFC in promoting Mus81-complex activity
SISÁKOVÁ, Alexandra, Veronika ALTMANNOVÁ, Marek ŠEBESTA a Lumír KREJČÍZákladní údaje
Originální název
Role of PCNA and RFC in promoting Mus81-complex activity
Autoři
SISÁKOVÁ, Alexandra (703 Slovensko, domácí), Veronika ALTMANNOVÁ (203 Česká republika, domácí), Marek ŠEBESTA (703 Slovensko, domácí) a Lumír KREJČÍ (203 Česká republika, garant, domácí)
Vydání
BMC BIOLOGY, LONDON, BIOMED CENTRAL LTD, 2017, 1741-7007
Další údaje
Jazyk
angličtina
Typ výsledku
Článek v odborném periodiku
Obor
10600 1.6 Biological sciences
Stát vydavatele
Velká Británie a Severní Irsko
Utajení
není předmětem státního či obchodního tajemství
Impakt faktor
Impact factor: 5.770
Kód RIV
RIV/00216224:14110/17:00095209
Organizační jednotka
Lékařská fakulta
UT WoS
000412075900002
Klíčová slova anglicky
Replication factor C; Proliferating cell nuclear antigen; Mus81 complex; Replication; Recombination
Příznaky
Mezinárodní význam, Recenzováno
Změněno: 18. 3. 2018 16:47, Soňa Böhmová
Anotace
V originále
Background: Proper DNA replication is essential for faithful transmission of the genome. However, replication stress has serious impact on the integrity of the cell, leading to stalling or collapse of replication forks, and has been determined as a driving force of carcinogenesis. Mus81-Mms4 complex is a structure-specific endonuclease previously shown to be involved in processing of aberrant replication intermediates and promotes POLD3-dependent DNA synthesis via break-induced replication. However, how replication components might be involved in this process is not known. Results: Herein, we show the interaction and robust stimulation of Mus81-Mms4 nuclease activity by heteropentameric replication factor C(RFC) complex, the processivity factor of replicative DNA polymerases that is responsible for loading of proliferating cell nuclear antigen (PCNA) during DNA replication and repair. This stimulation is enhanced by RFC-dependent ATP hydrolysis and by PCNA loading on the DNA. Moreover, this stimulation is not specific to Rfc1, the largest of subunit of this complex, thus indicating that alternative clamp loaders may also play a role in the stimulation. We also observed a targeting of Mus81 by RFC to the nick-containing DNA substrate and we provide further evidence that indicates cooperation between Mus81 and the RFC complex in the repair of DNA lesions generated by various DNA-damaging agents. Conclusions: Identification of new interacting partners and modulators of Mus81-Mms4 nuclease, RFC, and PCNA imply the cooperation of these factors in resolution of stalled replication forks and branched DNA structures emanating from the restarted replication forks under conditions of replication stress.
Návaznosti
GAP207/12/2323, projekt VaV |
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GA13-26629S, projekt VaV |
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MUNI/M/1894/2014, interní kód MU |
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