Shi I, et al. (2009) Role of the Rad52 Amino-terminal DNA Binding Activity in DNA Strand Capture in Homologous Recombination. J Biol Chem 284(48):33275-84
Abstract: Saccharomyces cerevisiae Rad52 protein promotes homologous recombination by nucleating the Rad51 recombinase onto RPA-coated ssDNA strands and also by directly annealing such strands. We show that the purified rad52-R70A mutant protein, with a compromised amino-terminal DNA binding domain, is capable of Rad51 delivery to DNA, but is deficient in DNA annealing. Results from chromatin immunoprecipitation experiments find that rad52-R70A associates with DNA double strand breaks and promotes recruitment of Rad51 as efficiently as wild-type Rad52. Analysis of gene conversion intermediates reveals that rad52-R70A cells can mediate DNA strand invasion but are unable to complete the recombination event. These results provide evidence that DNA binding by the evolutionarily conserved amino-terminus of Rad52 is needed for the capture of the second DNA end during homologous recombination.
|Status: Published||Type: Journal Article||PubMed ID: 19812039|
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