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@article{1306994,
author = {Chavdarova, Melita and Marini Palomeque, María Victoria and Sisáková, Alexandra and Sedláčková, Hana and Vigašová, Dana and Brill, Steven J. and Lisby, Michael and Krejčí, Lumír},
article_location = {Oxford},
article_number = {7},
doi = {http://dx.doi.org/10.1093/nar/gkv198},
keywords = {SACCHAROMYCES-CEREVISIAE SRS2; POSTREPLICATION REPAIR PATHWAY; RAD51 PRESYNAPTIC FILAMENT; DOUBLE-STRAND BREAKS; HOMOLOGOUS RECOMBINATION; DNA HELICASE; REPLICATION FORKS; FISSION YEAST; MITOTIC RECOMBINATION; CELL-CYCLE},
language = {eng},
issn = {0305-1048},
journal = {Nucleic Acids Research},
title = {Srs2 promotes Mus81-Mms4-mediated resolution of recombination intermediates},
volume = {43},
year = {2015}
}
TY - JOUR
ID - 1306994
AU - Chavdarova, Melita - Marini Palomeque, María Victoria - Sisáková, Alexandra - Sedláčková, Hana - Vigašová, Dana - Brill, Steven J. - Lisby, Michael - Krejčí, Lumír
PY - 2015
TI - Srs2 promotes Mus81-Mms4-mediated resolution of recombination intermediates
JF - Nucleic Acids Research
VL - 43
IS - 7
SP - 3626-3642
EP - 3626-3642
PB - Oxford Press
SN - 03051048
KW - SACCHAROMYCES-CEREVISIAE SRS2
KW - POSTREPLICATION REPAIR PATHWAY
KW - RAD51 PRESYNAPTIC FILAMENT
KW - DOUBLE-STRAND BREAKS
KW - HOMOLOGOUS RECOMBINATION
KW - DNA HELICASE
KW - REPLICATION FORKS
KW - FISSION YEAST
KW - MITOTIC RECOMBINATION
KW - CELL-CYCLE
N2 - 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.
ER -
CHAVDAROVA, Melita, María Victoria MARINI PALOMEQUE, Alexandra SISÁKOVÁ, Hana SEDLÁČKOVÁ, Dana VIGAŠOVÁ, Steven J. BRILL, Michael LISBY and Lumír KREJČÍ. Srs2 promotes Mus81-Mms4-mediated resolution of recombination intermediates. \textit{Nucleic Acids Research}. Oxford: Oxford Press, 2015, vol.~43, No~7, p.~3626-3642. ISSN~0305-1048. Available from: https://dx.doi.org/10.1093/nar/gkv198.
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