Localization of recombination proteins and Srs2 reveals anti-recombinase function in vivo

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Publikace nespadá pod Filozofickou fakultu, ale pod Přírodovědeckou fakultu. Oficiální stránka publikace je na webu muni.cz.
Název česky Lokalizace rekombinčních proteinů a Srs2 odhalilo proti-rekombinační funkci in vivo
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BURGESS R.C. LISBY Michael ALTMANNOVÁ Veronika KREJČÍ Lumír SUNG Patrick ROTHSTEIN Rodney

Rok publikování 2009
Druh Článek v odborném periodiku
Časopis / Zdroj Journal of Cell Biology
Fakulta / Pracoviště MU

Přírodovědecká fakulta

Citace
Obor Genetika a molekulární biologie
Klíčová slova Homologous recombination; Srs2 anti-recombinase; Rad51 filaments; Rad54; Rad52; Replication fork
Popis Homologous recombination (HR), while an important DNA repair mechanism, is dangerous to the cell if improperly regulated. The Srs2 anti-recombinase restricts HR by disassembling the Rad51 nucleoprotein filament, an intermediate in homology search and exchange of homologous DNA strands. Here, through characterization of Srs2 function in vivo, we describe a novel mechanism for regulating the initiation of HR. We find that Srs2 is recruited separately to replication and repair centers, and describe the genetic requirements for its recruitment. In the absence of Srs2 activity, Rad51 foci accumulate, and surprisingly, these foci form in the absence of Rad52 mediation. However, these Rad51 foci do not represent repair proficient filaments as determined by recombination assays. Such antagonistic roles for Rad52 and Srs2 in Rad51 filament formation are also observed in vitro. Furthermore, we provide evidence that Srs2 removes Rad51 indiscriminately from DNA, while other HR proteins, particularly Rad52, coordinates appropriate filament reformation. This constant breakdown and rebuilding of filaments may act as a stringent quality control mechanism during HR.
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