Coordinated response of mammalian Rad51 and Rad52 to DNA damage.
Biochemical analysis has shown that mammalian Rad51 and Rad52 interact and synergize in DNA recombination reactions in vitro, but these proteins have not been shown to function together in response to DNA damage in vivo. By analysis of murine cells expressing murine Rad52 tagged with green fluorescent protein (GFP)-Rad52, we now show that DNA damage causes Rad51 and GFP-Rad52 to colocalize in distinct nuclear foci. Cells expressing GFP-Rad52 show both increased survival and an increased number of Rad51 foci, raising the possibility that Rad52 is limiting for repair. These observations provide evidence of coordinated function of Rad51 and Rad52 in vivo and support the hypothesis that Rad52 plays an important role in the DNA damage response in mammalian cells.
Liu
Y
Y
Department of Molecular Biophysics, Yale University School of Medicine, New Haven, CT 06520-8024, USA.
Maizels
N
N
D000818:Animals; D018906:Antineoplastic Agents, Alkylating / Q000494:pharmacology; D002460:Cell Line; D002467:Cell Nucleus / Q000187:drug effects / Q000378:metabolism* / Q000528:radiation effects; D002470:Cell Survival; D004249:DNA Damage; D004254:DNA Nucleotidyltransferases / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000378:metabolism*; D005786:Gene Expression Regulation; D017930:Genes, Reporter; D006801:Humans; D007259:Infrared Rays; D008741:Methyl Methanesulfonate / Q000494:pharmacology; D051379:Mice; D008856:Microscopy, Fluorescence; D051135:Rad51 Recombinase; D051721:Rad52 DNA Repair and Recombination Protein; D011993:Recombinant Fusion Proteins / Q000378:metabolism
D018906:Antineoplastic Agents, Alkylating; D004268:DNA-Binding Proteins; C497194:RAD52 protein, human; D051721:Rad52 DNA Repair and Recombination Protein; C497196:Rad52 protein, mouse; D011993:Recombinant Fusion Proteins; D008741:Methyl Methanesulfonate; D004254:DNA Nucleotidyltransferases; C495153:RAD51 protein, human; D051135:Rad51 Recombinase; C495154:Rad51 protein, mouse