Localization of recombination proteins and Srs2 reveals anti-recombinase function in vivo
BURGESS, R.C., Michael LISBY, Veronika ALTMANNOVÁ, Lumír KREJČÍ, Patrick SUNG and Rodney ROTHSTEIN. Localization of recombination proteins and Srs2 reveals anti-recombinase function in vivo. Journal of Cell Biology. 2009, vol. 185, No 6, p. 969-981, 12 pp. ISSN 0021-9525. |
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Original name | Localization of recombination proteins and Srs2 reveals anti-recombinase function in vivo |
Name in Czech | Lokalizace rekombinčních proteinů a Srs2 odhalilo proti-rekombinační funkci in vivo |
Authors | BURGESS, R.C. (840 United States of America), Michael LISBY (208 Denmark), Veronika ALTMANNOVÁ (203 Czech Republic), Lumír KREJČÍ (203 Czech Republic, guarantor), Patrick SUNG (840 United States of America) and Rodney ROTHSTEIN (840 United States of America). |
Edition | Journal of Cell Biology, 2009, 0021-9525. |
Other information | |
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Original language | English |
Type of outcome | Article in a journal |
Field of Study | Genetics and molecular biology |
Country of publisher | United States of America |
Confidentiality degree | is not subject to a state or trade secret |
Impact factor | Impact factor: 9.575 |
RIV identification code | RIV/00216224:14310/09:00029285 |
Organization unit | Faculty of Science |
UT WoS | 000267134000007 |
Keywords in English | Homologous recombination; Srs2 anti-recombinase; Rad51 filaments; Rad54; Rad52; Replication fork |
Tags | HOMOLOGOUS RECOMBINATION, Rad51 filaments, Rad52, Rad54, Replication fork, Srs2 anti-recombinase |
Tags | International impact, Reviewed |
Changed by | Changed by: doc. Mgr. Lumír Krejčí, Ph.D., učo 18098. Changed: 1/7/2009 08:06. |
Abstract |
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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. |
Abstract (in Czech) |
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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. |
Links | |
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GA301/09/1917, research and development project | Name: Štěpení replikačních-rekombinačních DNA meziproduktů a jejich úloha při nestabilitě genomu |
Investor: Czech Science Foundation | |
GD203/09/H046, research and development project | Name: Biochemie na rozcestí mezi in silico a in vitro |
Investor: Czech Science Foundation | |
LC06030, research and development project | Name: Biomolekulární centrum |
Investor: Ministry of Education, Youth and Sports of the CR, Biomolecular centre | |
MSM0021622413, plan (intention) | Name: Proteiny v metabolismu a při interakci organismů s prostředím |
Investor: Ministry of Education, Youth and Sports of the CR, Proteins in metabolism and interaction of organisms with the environment |
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