Detailed Information on Publication Record
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.Basic information
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
Language
English
Type of outcome
Článek v odborném periodiku
Field of Study
Genetics and molecular biology
Country of publisher
United States of America
Confidentiality degree
není předmětem státního či obchodního tajemství
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
Tags
International impact, Reviewed
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.
In Czech
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
| GA301/09/1917, research and development project |
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| GD203/09/H046, research and development project |
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| LC06030, research and development project |
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| MSM0021622413, plan (intention) |
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