2009
Localization of recombination proteins and Srs2 reveals anti-recombinase function in vivo
BURGESS, R.C., Michael LISBY, Veronika ALTMANNOVÁ, Lumír KREJČÍ, Patrick SUNG et. al.Základní údaje
Originální název
Localization of recombination proteins and Srs2 reveals anti-recombinase function in vivo
Název česky
Lokalizace rekombinčních proteinů a Srs2 odhalilo proti-rekombinační funkci in vivo
Autoři
BURGESS, R.C. (840 Spojené státy), Michael LISBY (208 Dánsko), Veronika ALTMANNOVÁ (203 Česká republika), Lumír KREJČÍ (203 Česká republika, garant), Patrick SUNG (840 Spojené státy) a Rodney ROTHSTEIN (840 Spojené státy)
Vydání
Journal of Cell Biology, 2009, 0021-9525
Další údaje
Jazyk
angličtina
Typ výsledku
Článek v odborném periodiku
Obor
Genetika a molekulární biologie
Stát vydavatele
Spojené státy
Utajení
není předmětem státního či obchodního tajemství
Impakt faktor
Impact factor: 9.575
Kód RIV
RIV/00216224:14310/09:00029285
Organizační jednotka
Přírodovědecká fakulta
UT WoS
000267134000007
Klíčová slova anglicky
Homologous recombination; Srs2 anti-recombinase; Rad51 filaments; Rad54; Rad52; Replication fork
Štítky
Příznaky
Mezinárodní význam, Recenzováno
Změněno: 1. 7. 2009 08:06, doc. Mgr. Lumír Krejčí, Ph.D.
V originále
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.
Česky
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.
Návaznosti
| GA301/09/1917, projekt VaV |
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| GD203/09/H046, projekt VaV |
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| LC06030, projekt VaV |
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| MSM0021622413, záměr |
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