KOLESÁR, Peter, Prabha SARANGI, Veronika ALTMANNOVÁ, Xiaolan ZHAO a Lumír KREJČÍ. Dual roles of the SUMO-interacting motif in the regulation of Srs2 sumoylation. Nucleic Acids Research. Oxford: Oxford University Press, 2012, roč. 40, č. 16, s. 7831-7843. ISSN 0305-1048. Dostupné z: https://dx.doi.org/10.1093/nar/gks484. |
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@article{1066872, author = {Kolesár, Peter and Sarangi, Prabha and Altmannová, Veronika and Zhao, Xiaolan and Krejčí, Lumír}, article_location = {Oxford}, article_number = {16}, doi = {http://dx.doi.org/10.1093/nar/gks484}, keywords = {Srs2 SUMO PCNA}, language = {eng}, issn = {0305-1048}, journal = {Nucleic Acids Research}, title = {Dual roles of the SUMO-interacting motif in the regulation of Srs2 sumoylation.}, url = {http://nar.oxfordjournals.org/content/40/16/7831.long}, volume = {40}, year = {2012} }
TY - JOUR ID - 1066872 AU - Kolesár, Peter - Sarangi, Prabha - Altmannová, Veronika - Zhao, Xiaolan - Krejčí, Lumír PY - 2012 TI - Dual roles of the SUMO-interacting motif in the regulation of Srs2 sumoylation. JF - Nucleic Acids Research VL - 40 IS - 16 SP - 7831-7843 EP - 7831-7843 PB - Oxford University Press SN - 03051048 KW - Srs2 SUMO PCNA UR - http://nar.oxfordjournals.org/content/40/16/7831.long L2 - http://nar.oxfordjournals.org/content/40/16/7831.long N2 - 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. These two functions of Srs2's SIM exhibit a competitive relationship: sumoylation of Srs2 decreases the interaction between the SIM and SUMO-PCNA, and the SUMO-PCNA-SIM interaction disfavors Srs2 sumoylation. Our findings suggest a potential mechanism for the equilibrium of sumoylated and PCNA-bound pools of Srs2 in cells. ER -
KOLESÁR, Peter, Prabha SARANGI, Veronika ALTMANNOVÁ, Xiaolan ZHAO a Lumír KREJČÍ. Dual roles of the SUMO-interacting motif in the regulation of Srs2 sumoylation. \textit{Nucleic Acids Research}. Oxford: Oxford University Press, 2012, roč.~40, č.~16, s.~7831-7843. ISSN~0305-1048. Dostupné z: https://dx.doi.org/10.1093/nar/gks484.
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