2015
Srs2 promotes Mus81-Mms4-mediated resolution of recombination intermediates
CHAVDAROVA, Melita; María Victoria MARINI PALOMEQUE; Alexandra SISÁKOVÁ; Hana SEDLÁČKOVÁ; Dana VIGAŠOVÁ et al.Základní údaje
Originální název
Srs2 promotes Mus81-Mms4-mediated resolution of recombination intermediates
Autoři
CHAVDAROVA, Melita; María Victoria MARINI PALOMEQUE; Alexandra SISÁKOVÁ; Hana SEDLÁČKOVÁ; Dana VIGAŠOVÁ; Steven J. BRILL; Michael LISBY a Lumír KREJČÍ
Vydání
Nucleic Acids Research, Oxford, Oxford Press, 2015, 0305-1048
Další údaje
Jazyk
angličtina
Typ výsledku
Článek v odborném periodiku
Obor
Genetika a molekulární biologie
Stát vydavatele
Velká Británie a Severní Irsko
Utajení
není předmětem státního či obchodního tajemství
Impakt faktor
Impact factor: 9.202
Označené pro přenos do RIV
Ano
Kód RIV
RIV/00216224:14110/15:00080935
Organizační jednotka
Lékařská fakulta
UT WoS
EID Scopus
Klíčová slova anglicky
SACCHAROMYCES-CEREVISIAE SRS2; POSTREPLICATION REPAIR PATHWAY; RAD51 PRESYNAPTIC FILAMENT; DOUBLE-STRAND BREAKS; HOMOLOGOUS RECOMBINATION; DNA HELICASE; REPLICATION FORKS; FISSION YEAST; MITOTIC RECOMBINATION; CELL-CYCLE
Příznaky
Mezinárodní význam, Recenzováno
Změněno: 29. 7. 2015 12:36, Ing. Mgr. Věra Pospíšilíková
Anotace
V originále
A variety of DNA lesions, secondary DNA structures or topological stress within the DNA template may lead to stalling of the replication fork. Recovery of such forks is essential for the maintenance of genomic stability. The structure-specific endonuclease Mus81-Mms4 has been implicated in processing DNA intermediates that arise from collapsed forks and homologous recombination. According to previous genetic studies, the Srs2 helicase may play a role in the repair of double-strand breaks and ssDNA gaps together with Mus81-Mms4. In this study, we show that the Srs2 and Mus81-Mms4 proteins physically interact in vitro and in vivo and we map the interaction domains within the Srs2 and Mus81 proteins. Further, we show that Srs2 plays a dual role in the stimulation of the Mus81-Mms4 nuclease activity on a variety of DNA substrates. First, Srs2 directly stimulates Mus81-Mms4 nuclease activity independent of its helicase activity. Second, Srs2 removes Rad51 from DNA to allow access of Mus81-Mms4 to cleave DNA. Concomitantly, Mus81-Mms4 inhibits the helicase activity of Srs2. Taken together, our data point to a coordinated role of Mus81-Mms4 and Srs2 in processing of recombination as well as replication intermediates.
Návaznosti
| GAP207/12/2323, projekt VaV |
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| GA13-26629S, projekt VaV |
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