Strand exchange activity of human recombination protein Rad52
AUTOR(ES)
Kumar, Jaspal K.
FONTE
National Academy of Sciences
RESUMO
Repair of double-strand breaks is essential for the maintenance of genome integrity and cell survival. In eukaryotes, double-strand-break repair by homologous recombination requires the Rad52 group of proteins. Human Rad52 protein (HsRad52)-mediated annealing of complementary strands has been studied in detail, but little has been reported on the recombinase activities of HsRad52. For this study, we purified HsRad52 from Escherichia coli. DNase I protection experiments indicated that HsRad52 binds preferentially to single-stranded DNA and protects it against digestion by DNase I. HsRad52 catalyzed D-loop formation in superhelical DNA, as well as strand exchange among oligonucleotide substrates. The formation of a stoichiometric complex between HsRad52 and single-stranded DNA was found to be critical for strand exchange activity, and the coating of both the single- and double-stranded oligonucleotides inhibited the exchange reaction.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=470714Documentos Relacionados
- Human and yeast Rad52 proteins promote DNA strand exchange
- Structure of the single-strand annealing domain of human RAD52 protein
- Overexpression of human RAD51 and RAD52 reduces double-strand break-induced homologous recombination in mammalian cells
- Role of the Rad52 Amino-terminal DNA Binding Activity in DNA Strand Capture in Homologous Recombination*
- DNA strand annealing is promoted by the yeast Rad52 protein.
