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Unwinding of synthetic replication and recombination substrates by Srs2

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F12%3A00057534" target="_blank" >RIV/00216224:14310/12:00057534 - isvavai.cz</a>

  • Alternative codes found

    RIV/00159816:_____/12:#0000964

  • Result on the web

    <a href="http://dx.doi.org/10.1016/j.dnarep.2012.05.007" target="_blank" >http://dx.doi.org/10.1016/j.dnarep.2012.05.007</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.dnarep.2012.05.007" target="_blank" >10.1016/j.dnarep.2012.05.007</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Unwinding of synthetic replication and recombination substrates by Srs2

  • Original language description

    The budding yeast Srs2 protein possesses 3 to 5 DNA helicase activity and channels untimely recombination to post-replication repair by removing Rad51 from ssDNA. However, it also promotes recombination via a synthesis-dependent strand-annealing pathway(SDSA). Furthermore, at the replication fork, Srs2 is required for fork progression and prevents the instability of trinucleotide repeats. To better understand the multiple roles of the Srs2 helicase during these processes, we analysed the ability of Srs2 to bind and unwind various DNA substrates that mimic structures present during DNA replication and recombination. While leading or lagging strands were efficiently unwound, the presence of ssDNA binding protein RPA presented an obstacle for Srs2 translocation. We also tested the preferred directionality of unwinding of various substrates and studied the effect of Rad51 and Mre11 proteins on Srs2 helicase activity.

  • 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)

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

    DNA Repair

  • ISSN

    1568-7864

  • e-ISSN

  • Volume of the periodical

    11

  • Issue of the periodical within the volume

    10

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    10

  • Pages from-to

    789-798

  • UT code for WoS article

    000310761100002

  • EID of the result in the Scopus database