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.Základní údaje
Originální název
Interaction with RPA Is Necessary for Rad52 Repair Center Formation and for Its Mediator Activity.
Název česky
Interakce s RPA je nezbytná pro vznik Rad52 opravného centra a jeho mediátorové aktivity
Autoři
PLATE, Iben (208 Dánsko), SC HALLWYL (208 Dánsko), Idina SHI (840 Spojené státy), Lumir KREJCI (203 Česká republika, garant), C. MULLER (208 Dánsko), L. ALBERTSEN (208 Dánsko), Patrick SUNG (840 Spojené státy) a Uffe MORTENSEN (208 Dánsko)
Vydání
J. Biol. Chem. 2008, 0021-9258
Další údaje
Jazyk
angličtina
Typ výsledku
Článek v odborném periodiku
Obor
10600 1.6 Biological sciences
Stát vydavatele
Spojené státy
Utajení
není předmětem státního či obchodního tajemství
Odkazy
Impakt faktor
Impact factor: 5.520
Kód RIV
RIV/00216224:14310/08:00026744
Organizační jednotka
Přírodovědecká fakulta
UT WoS
000260179900035
Klíčová slova anglicky
Rad52; recombination mediator; DNA repair
Štítky
Příznaky
Mezinárodní význam, Recenzováno
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.
Česky
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.
Návaznosti
| LC06030, projekt VaV |
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| ME 888, projekt VaV |
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| MSM0021622413, záměr |
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