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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