Detailed Information on Publication Record
2008
Interaction with RPA Is Necessary for Rad52 Repair Center Formation and for Its Mediator Activity.
PLATE, Iben, SC HALLWYL, Idina SHI, Lumir KREJCI, C. MULLER et. al.Basic information
Original name
Interaction with RPA Is Necessary for Rad52 Repair Center Formation and for Its Mediator Activity.
Name in Czech
Interakce s RPA je nezbytná pro vznik Rad52 opravného centra a jeho mediátorové aktivity
Authors
PLATE, Iben (208 Denmark), SC HALLWYL (208 Denmark), Idina SHI (840 United States of America), Lumir KREJCI (203 Czech Republic, guarantor), C. MULLER (208 Denmark), L. ALBERTSEN (208 Denmark), Patrick SUNG (840 United States of America) and Uffe MORTENSEN (208 Denmark)
Edition
J. Biol. Chem. 2008, 0021-9258
Other information
Language
English
Type of outcome
Článek v odborném periodiku
Field of Study
10600 1.6 Biological sciences
Country of publisher
United States of America
Confidentiality degree
není předmětem státního či obchodního tajemství
References:
Impact factor
Impact factor: 5.520
RIV identification code
RIV/00216224:14310/08:00026744
Organization unit
Faculty of Science
UT WoS
000260179900035
Keywords in English
Rad52; recombination mediator; DNA repair
Tags
International impact, Reviewed
Změněno: 24/6/2009 07:34, doc. Mgr. Lumír Krejčí, Ph.D.
V originále
Homologous recombination (HR) is a major DNA repair pathway and therefore essential for maintaining the integrity of the genome. HR is catalyzed by proteins encoded by genes of the RAD52 epistasis group, including the recombinase Rad51 and its mediator Rad52. HR proteins fused with green fluorescent protein form foci at damaged DNA reflecting the assembly of repair centers that harbor a high concentration of repair proteins. Rad52 mediates the recruitment of Rad51 and other HR proteins to DNA damage. To understand the mechanism for the assembly of Rad52-dependent DNA repair centers, we used a mutational strategy to identify a Rad52 domain essential for its recruitment to DNA repair foci. We present evidence to implicate an acidic domain in Rad52 in DNA repair focus formation. Mutations in this domain confer marked DNA damage sensitivity and recombination deficiency. Importantly, these Rad52 mutants are specifically compromised for interaction with the single-stranded DNA-binding factor RPA. Based on these findings, we propose a model where Rad52 displaces RPA from single-stranded DNA using the acidic domain as a molecular lever.
In Czech
Homologous recombination (HR) is a major DNA repair pathway and therefore essential for maintaining the integrity of the genome. HR is catalyzed by proteins encoded by genes of the RAD52 epistasis group, including the recombinase Rad51 and its mediator Rad52. HR proteins fused with green fluorescent protein form foci at damaged DNA reflecting the assembly of repair centers that harbor a high concentration of repair proteins. Rad52 mediates the recruitment of Rad51 and other HR proteins to DNA damage. To understand the mechanism for the assembly of Rad52-dependent DNA repair centers, we used a mutational strategy to identify a Rad52 domain essential for its recruitment to DNA repair foci. We present evidence to implicate an acidic domain in Rad52 in DNA repair focus formation. Mutations in this domain confer marked DNA damage sensitivity and recombination deficiency. Importantly, these Rad52 mutants are specifically compromised for interaction with the single-stranded DNA-binding factor RPA. Based on these findings, we propose a model where Rad52 displaces RPA from single-stranded DNA using the acidic domain as a molecular lever.
Links
| LC06030, research and development project |
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| ME 888, research and development project |
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| MSM0021622413, plan (intention) |
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