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Statements

Subject Item
n2:RIV%2F00216224%3A14110%2F12%3A00057621%21RIV13-GA0-14110___
rdf:type
skos:Concept n20:Vysledek
rdfs:seeAlso
http://nar.oxfordjournals.org/content/40/16/7831.long
dcterms:description
The Srs2 DNA helicase of Saccharomyces cerevisiae affects recombination in multiple ways. Srs2 not only inhibits recombination at stalled replication forks but also promotes the synthesis-dependent strand annealing (SDSA) pathway of recombination. Both functions of Srs2 are regulated by sumoylation-sumoylated PCNA recruits Srs2 to the replication fork to disfavor recombination, and sumoylation of Srs2 can be inhibitory to SDSA in certain backgrounds. To understand Srs2 function, we characterize the mechanism of its sumoylation in vitro and in vivo. Our data show that Srs2 is sumoylated at three lysines, and its sumoylation is facilitated by the Siz SUMO ligases. We also show that Srs2 binds to SUMO via a C-terminal SUMO-interacting motif (SIM). The SIM region is required for Srs2 sumoylation, likely by binding to SUMO-charged Ubc9. Srs2's SIM also cooperates with an adjacent PCNA-specific interaction site in binding to sumoylated PCNA to ensure the specificity of the interaction. The Srs2 DNA helicase of Saccharomyces cerevisiae affects recombination in multiple ways. Srs2 not only inhibits recombination at stalled replication forks but also promotes the synthesis-dependent strand annealing (SDSA) pathway of recombination. Both functions of Srs2 are regulated by sumoylation-sumoylated PCNA recruits Srs2 to the replication fork to disfavor recombination, and sumoylation of Srs2 can be inhibitory to SDSA in certain backgrounds. To understand Srs2 function, we characterize the mechanism of its sumoylation in vitro and in vivo. Our data show that Srs2 is sumoylated at three lysines, and its sumoylation is facilitated by the Siz SUMO ligases. We also show that Srs2 binds to SUMO via a C-terminal SUMO-interacting motif (SIM). The SIM region is required for Srs2 sumoylation, likely by binding to SUMO-charged Ubc9. Srs2's SIM also cooperates with an adjacent PCNA-specific interaction site in binding to sumoylated PCNA to ensure the specificity of the interaction.
dcterms:title
Dual roles of the SUMO-interacting motif in the regulation of Srs2 sumoylation. Dual roles of the SUMO-interacting motif in the regulation of Srs2 sumoylation.
skos:prefLabel
Dual roles of the SUMO-interacting motif in the regulation of Srs2 sumoylation. Dual roles of the SUMO-interacting motif in the regulation of Srs2 sumoylation.
skos:notation
RIV/00216224:14110/12:00057621!RIV13-GA0-14110___
n20:predkladatel
n21:orjk%3A14110
n3:aktivita
n10:S n10:P n10:Z
n3:aktivity
P(ED1.100/02/0123), P(EE2.3.09.0186), P(GA301/09/1917), P(GAP207/12/2323), P(GD203/09/H046), P(LC06030), P(ME10048), S, Z(MSM0021622413)
n3:cisloPeriodika
16
n3:dodaniDat
n9:2013
n3:domaciTvurceVysledku
n13:2565277 n13:6938566 n13:4160517
n3:druhVysledku
n14:J
n3:duvernostUdaju
n17:S
n3:entitaPredkladatele
n6:predkladatel
n3:idSjednocenehoVysledku
132283
n3:idVysledku
RIV/00216224:14110/12:00057621
n3:jazykVysledku
n4:eng
n3:klicovaSlova
Srs2 SUMO PCNA
n3:klicoveSlovo
n8:Srs2%20SUMO%20PCNA
n3:kodStatuVydavatele
CZ - Česká republika
n3:kontrolniKodProRIV
[53AB92750298]
n3:nazevZdroje
Nucleic Acids Research
n3:obor
n5:CE
n3:pocetDomacichTvurcuVysledku
3
n3:pocetTvurcuVysledku
5
n3:projekt
n7:ED1.100%2F02%2F0123 n7:GAP207%2F12%2F2323 n7:EE2.3.09.0186 n7:ME10048 n7:GD203%2F09%2FH046 n7:GA301%2F09%2F1917 n7:LC06030
n3:rokUplatneniVysledku
n9:2012
n3:svazekPeriodika
40
n3:tvurceVysledku
Kolesár, Peter Sarangi, Prabha Altmannová, Veronika Zhao, Xiaolan Krejčí, Lumír
n3:wos
000308959800028
n3:zamer
n18:MSM0021622413
s:issn
0305-1048
s:numberOfPages
13
n12:doi
10.1093/nar/gks484
n11:organizacniJednotka
14110