About: Dual roles of the SUMO-interacting motif in the regulation of Srs2 sumoylation.

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About: Dual roles of the SUMO-interacting motif in the regulation of Srs2 sumoylation. Goto Sponge Distinct Permalink

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Attributes	Values
rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
rdfs:seeAlso	http://nar.oxfordjournals.org/content/40/16/7831.long
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. (en)
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. (en)
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. (en)
skos:notation	RIV/00216224:14110/12:00057621!RIV13-GA0-14110___
http://linked.open...avai/riv/aktivita	P S Z
http://linked.open...avai/riv/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)
http://linked.open...iv/cisloPeriodika	16
http://linked.open...vai/riv/dodaniDat	2013
http://linked.open...aciTvurceVysledku	Krejčí, Lumír Altmannová, Veronika Kolesár, Peter
http://linked.open.../riv/druhVysledku	J - Článek v odborném periodiku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Masarykova univerzita / Lékařská fakulta
http://linked.open...dnocenehoVysledku	132283
http://linked.open...ai/riv/idVysledku	RIV/00216224:14110/12:00057621
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	Srs2 SUMO PCNA (en)
http://linked.open.../riv/klicoveSlovo	Srs2 SUMO PCNA
http://linked.open...odStatuVydavatele	CZ - Česká republika
http://linked.open...ontrolniKodProRIV	[53AB92750298]
http://linked.open...i/riv/nazevZdroje	Nucleic Acids Research
http://linked.open...in/vavai/riv/obor	CE
http://linked.open...ichTvurcuVysledku	3 (xsd:int)
http://linked.open...cetTvurcuVysledku	5 (xsd:int)
http://linked.open...vavai/riv/projekt	Biomolecular centre Biochemistry on the crossroad from in silico to in vitro Mendel Centre for Education in Biology, Biomedicine and Bioinformatics Endonuclease and translocase activity in type I restriction-modification complexes St. Anne´s University Hospital Brno - International Clinical Research Center (FNUSA-ICRC) Resolution of replication-recombination DNA intermediates and its role in genomic instability The role of post-translational modification in DNA repair and recombination: Meiosis, SUMOylation and Zip3 protein
http://linked.open...UplatneniVysledku	2012
http://linked.open...v/svazekPeriodika	40
http://linked.open...iv/tvurceVysledku	Krejčí, Lumír Altmannová, Veronika Kolesár, Peter Sarangi, Prabha Zhao, Xiaolan
http://linked.open...ain/vavai/riv/wos	000308959800028
http://linked.open...n/vavai/riv/zamer	Proteiny v metabolismu a při interakci organismů s prostředím
issn	0305-1048
number of pages	13 (xsd:int)
http://bibframe.org/vocab/doi	10.1093/nar/gks484
http://localhost/t...ganizacniJednotka	14110

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