| BURKOVICS, Peter, Marek ŠEBESTA, Alexandra SISÁKOVÁ, Nicolas PLAULT, Valeria SZUKACSOV, Thomas ROBERT, Lajos PINTER, María Victoria MARINI PALOMEQUE, Peter KOLESÁR, Lajos HARACSKA, Serge GANGLOFF a Lumír KREJČÍ. Srs2 mediates PCNA-SUMO-dependent inhibition of DNA repair synthesis. EMBO JOURNAL. NEW YORK: NATURE PUBLISHING GROUP, 2013, roč. 32, č. 5, s. 742-755. ISSN 0261-4189. Dostupné z: https://dx.doi.org/10.1038/emboj.2013.9. |
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@article{1124592,
author = {Burkovics, Peter and Šebesta, Marek and Sisáková, Alexandra and Plault, Nicolas and Szukacsov, Valeria and Robert, Thomas and Pinter, Lajos and Marini Palomeque, María Victoria and Kolesár, Peter and Haracska, Lajos and Gangloff, Serge and Krejčí, Lumír},
article_location = {NEW YORK},
article_number = {5},
doi = {http://dx.doi.org/10.1038/emboj.2013.9},
keywords = {DNA repair synthesis; genome stability; PCNA SUMOylation; Srs2; SUMO interacting motif},
language = {eng},
issn = {0261-4189},
journal = {EMBO JOURNAL},
title = {Srs2 mediates PCNA-SUMO-dependent inhibition of DNA repair synthesis},
volume = {32},
year = {2013}
}
TY - JOUR
ID - 1124592
AU - Burkovics, Peter - Šebesta, Marek - Sisáková, Alexandra - Plault, Nicolas - Szukacsov, Valeria - Robert, Thomas - Pinter, Lajos - Marini Palomeque, María Victoria - Kolesár, Peter - Haracska, Lajos - Gangloff, Serge - Krejčí, Lumír
PY - 2013
TI - Srs2 mediates PCNA-SUMO-dependent inhibition of DNA repair synthesis
JF - EMBO JOURNAL
VL - 32
IS - 5
SP - 742-755
EP - 742-755
PB - NATURE PUBLISHING GROUP
SN - 02614189
KW - DNA repair synthesis
KW - genome stability
KW - PCNA SUMOylation
KW - Srs2
KW - SUMO interacting motif
N2 - Completion of DNA replication needs to be ensured even when challenged with fork progression problems or DNA damage. PCNA and its modifications constitute a molecular switch to control distinct repair pathways. In yeast, SUMOylated PCNA (S-PCNA) recruits Srs2 to sites of replication where Srs2 can disrupt Rad51 filaments and prevent homologous recombination (HR). We report here an unexpected additional mechanism by which S-PCNA and Srs2 block the synthesis-dependent extension of a recombination intermediate, thus limiting its potentially hazardous resolution in association with a cross-over. This new Srs2 activity requires the SUMO interaction motif at its C-terminus, but neither its translocase activity nor its interaction with Rad51. Srs2 binding to S-PCNA dissociates Pol delta and Pol eta from the repair synthesis machinery, thus revealing a novel regulatory mechanism controlling spontaneous genome rearrangements. Our results suggest that cycling cells use the Siz1-dependent SUMOylation of PCNA to limit the extension of repair synthesis during template switch or HR and attenuate reciprocal DNA strand exchanges to maintain genome stability.
ER -
BURKOVICS, Peter, Marek ŠEBESTA, Alexandra SISÁKOVÁ, Nicolas PLAULT, Valeria SZUKACSOV, Thomas ROBERT, Lajos PINTER, María Victoria MARINI PALOMEQUE, Peter KOLESÁR, Lajos HARACSKA, Serge GANGLOFF a Lumír KREJČÍ. Srs2 mediates PCNA-SUMO-dependent inhibition of DNA repair synthesis. \textit{EMBO JOURNAL}. NEW YORK: NATURE PUBLISHING GROUP, 2013, roč.~32, č.~5, s.~742-755. ISSN~0261-4189. Dostupné z: https://dx.doi.org/10.1038/emboj.2013.9.
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