ArticleThe Journal of biological chemistry2011
Vital roles of the second DNA-binding site of Rad52 protein in yeast homologous recombination.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 20 citations in OpenAlex.
- Establishment of SRLC: a multiplex genome editing technology for Saccharomyces cerevisiae and its application in metabolic engineering of malonyl-CoA pathway.Microbial cell factories · 2026Article
- Monomers and short oligomers of human RAD52 promote single-strand annealing.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Yeast Rad52 is a homodecamer and possesses BRCA2-like bipartite Rad51 binding modes.Nature communications · 2023Article
- Homodecameric Rad52 promotes single-position Rad51 nucleation in homologous recombination.bioRxiv : the preprint server for biology · 2023Article
- Article
- Rad52 Inverse Strand Exchange Drives RNA-Templated DNA Double-Strand Break Repair.Molecular cell · 2017Article
- Rad51 and RecA juxtapose dsDNA ends ready for DNA ligase-catalyzed end-joining under recombinase-suppressive conditions.Nucleic acids research · 2017Article
- Review
- A Checkpoint-Related Function of the MCM Replicative Helicase Is Required to Avert Accumulation of RNA:DNA Hybrids during S-phase and Ensuing DSBs during G2/M.PLoS genetics · 2016Article
- Functional Validation of Rare Human Genetic Variants Involved in Homologous Recombination Using Saccharomyces cerevisiae.PloS one · 2015Article
- Loop L1 governs the DNA-binding specificity and order for RecA-catalyzed reactions in homologous recombination and DNA repair.Nucleic acids research · 2015Article
- Functional analyses of the C-terminal half of the Saccharomyces cerevisiae Rad52 protein.Nucleic acids research · 2014Article
- Putative antirecombinase Srs2 DNA helicase promotes noncrossover homologous recombination avoiding loss of heterozygosity.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Molecular pathways: understanding the role of Rad52 in homologous recombination for therapeutic advancement.Clinical cancer research : an official journal of the American Association for Cancer Research · 2012Review
- Regulatory mechanisms and clinical perspectives of miRNA in tumor radiosensitivity.Carcinogenesis · 2012Review
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
RecA/Rad51 proteins are essential in homologous DNA recombination and catalyze the ATP-dependent formation of D-loops from a single-stranded DNA and an internal homologous sequence in a double-stranded DNA. RecA and Rad51 require a "recombination mediator" to overcome the interference imposed by the prior binding of single-stranded binding protein/replication protein A to the single-stranded DNA. Rad52 is the prototype of recombination mediators, and the human Rad52 protein has two distinct DNA-binding sites: the first site binds to single-stranded DNA, and the second site binds to either double- or single-stranded DNA. We previously showed that yeast Rad52 extensively stimulates Rad51-catalyzed D-loop formation even in the absence of replication protein A, by forming a 2:1 stoichiometric complex with Rad51. However, the precise roles of Rad52 and Rad51 within the complex are unknown. In the present study, we constructed yeast Rad52 mutants in which the amino acid residues corresponding to the second DNA-binding site of the human Rad52 protein were replaced with either alanine or aspartic acid. We found that the second DNA-binding site is important for the yeast Rad52 function in vivo. Rad51-Rad52 complexes consisting of these Rad52 mutants were defective in promoting the formation of D-loops, and the ability of the complex to associate with double-stranded DNA was specifically impaired. Our studies suggest that Rad52 within the complex associates with double-stranded DNA to assist Rad51-mediated homologous pairing.
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