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

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14110%2F12%3A00057621" target="_blank" >RIV/00216224:14110/12:00057621 - isvavai.cz</a>

  • Alternative codes found

    RIV/00159816:_____/12:#0000940

  • Result on the web

    <a href="http://nar.oxfordjournals.org/content/40/16/7831.long" target="_blank" >http://nar.oxfordjournals.org/content/40/16/7831.long</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1093/nar/gks484" target="_blank" >10.1093/nar/gks484</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

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

  • Original language 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 SIMregion 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.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)<br>S - Specificky vyzkum na vysokych skolach

Others

  • Publication year

    2012

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Nucleic Acids Research

  • ISSN

    0305-1048

  • e-ISSN

  • Volume of the periodical

    40

  • Issue of the periodical within the volume

    16

  • Country of publishing house

    CZ - CZECH REPUBLIC

  • Number of pages

    13

  • Pages from-to

    7831-7843

  • UT code for WoS article

    000308959800028

  • EID of the result in the Scopus database