Detailed Information on Publication Record
2015
Srs2 promotes Mus81-Mms4-mediated resolution of recombination intermediates
CHAVDAROVA, Melita, María Victoria MARINI PALOMEQUE, Alexandra SISÁKOVÁ, Hana SEDLÁČKOVÁ, Dana VIGAŠOVÁ et. al.Basic information
Original name
Srs2 promotes Mus81-Mms4-mediated resolution of recombination intermediates
Authors
CHAVDAROVA, Melita (807 North Macedonia, belonging to the institution), María Victoria MARINI PALOMEQUE (858 Uruguay, belonging to the institution), Alexandra SISÁKOVÁ (703 Slovakia, belonging to the institution), Hana SEDLÁČKOVÁ (203 Czech Republic, belonging to the institution), Dana VIGAŠOVÁ (703 Slovakia, belonging to the institution), Steven J. BRILL (840 United States of America), Michael LISBY (208 Denmark) and Lumír KREJČÍ (203 Czech Republic, guarantor, belonging to the institution)
Edition
Nucleic Acids Research, Oxford, Oxford Press, 2015, 0305-1048
Other information
Language
English
Type of outcome
Článek v odborném periodiku
Field of Study
Genetics and molecular biology
Country of publisher
United Kingdom of Great Britain and Northern Ireland
Confidentiality degree
není předmětem státního či obchodního tajemství
Impact factor
Impact factor: 9.202
RIV identification code
RIV/00216224:14110/15:00080935
Organization unit
Faculty of Medicine
UT WoS
000354722500025
Keywords in English
SACCHAROMYCES-CEREVISIAE SRS2; POSTREPLICATION REPAIR PATHWAY; RAD51 PRESYNAPTIC FILAMENT; DOUBLE-STRAND BREAKS; HOMOLOGOUS RECOMBINATION; DNA HELICASE; REPLICATION FORKS; FISSION YEAST; MITOTIC RECOMBINATION; CELL-CYCLE
Tags
International impact, Reviewed
Změněno: 29/7/2015 12:36, Ing. Mgr. Věra Pospíšilíková
Abstract
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.
Links
GAP207/12/2323, research and development project |
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GA13-26629S, research and development project |
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