{"doi":"10.1016/j.jmb.2009.05.009","title":"Dynamic Regulatory Interactions of Rad51, Rad52, and Replication Protein-A in Recombination Intermediates","abstract":null,"journal":"Journal of Molecular Biology","year":2009,"id":614962,"datarank":0.5676284450877392,"base_score":3.784189633918261,"endowment":3.784189633918261,"self_citation_contribution":0.5676284450877392,"citation_network_contribution":0.0,"self_endowment_contribution":0.5676284450877392,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":43,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":1052495,"name":"Noriko Kantake","orcid":null,"position":1,"is_corresponding":false},{"id":753956,"name":"Tomohiko Sugiyama","orcid":"0000-0003-2942-3667","position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Dynamic Regulatory Interactions of Rad51, Rad52, and Replication Protein-A in Recombination Intermediates","abstract":"Rad51, Rad52, and replication protein-A (RPA) play crucial roles in the repair of DNA double-strand breaks in Saccharomyces cerevisiae. Rad51 mediates DNA strand exchange, a key reaction in DNA recombination. Rad52 recruits Rad51 into single-stranded DNAs (ssDNAs) that are saturated with RPA. Rad52 also promotes annealing of ssDNA strands that are complexed with RPA. Specific protein-protein interactions are involved in these reactions. Here we report new biochemical characteristics of these protein interactions. First, Rad52-RPA interaction requires multiple molecules of RPA to be associated with ssDNA, suggesting that multiple contacts between the Rad52 ring and RPA-ssDNA filament are needed for stable binding. Second, RPA-t11, which is a recombination-deficient mutant of RPA, displays a defect in interacting with Rad52 in the presence of salt above 50 mM, explaining the defect in Rad52-mediated ssDNA annealing in the presence of this mutation. Third, ssDNA annealing promoted by Rad52 is preceded by aggregation of multiple RPA-ssDNA complexes with Rad52, and Rad51 inhibits this aggregation. These results suggest a regulatory role for Rad51 that suppresses ssDNA annealing and facilitates DNA strand invasion. Finally, the Rad51-double-stranded DNA complex disrupts Rad52-RPA interaction in ssDNA and titrates Rad52 from RPA. This suggests an additional regulatory role for Rad51 following DNA strand invasion, where Rad51-double-stranded DNA may inhibit illegitimate second-end capture to ensure the error-free repair of a DNA double-strand break.","is_dataset_classified":null,"base_score":3.784189633918261,"endowment":3.784189633918261,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"19445949","pmcid":null,"openalex_id":"https://openalex.org/W2057673816","authors":[],"funders":[],"total_grants":0,"fwci":1.3851,"citation_percentile":0.79934529,"influential_citations":0,"citation_trend":[{"year":2012,"count":4},{"year":2013,"count":3},{"year":2014,"count":3},{"year":2015,"count":1},{"year":2016,"count":5},{"year":2017,"count":4},{"year":2018,"count":1},{"year":2019,"count":5},{"year":2020,"count":4},{"year":2021,"count":2},{"year":2022,"count":2},{"year":2023,"count":1},{"year":2024,"count":1}],"oa_status":"closed","license":"https://www.elsevier.com/tdm/userlicense/1.0/","oa_locations":[{"url":"https://api.elsevier.com/content/article/PII:S0022283609005737?httpAccept=text/xml","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S0022283609005737?httpAccept=text/plain","host_type":"publisher"},{"url":"https://doi.org/10.1016/j.jmb.2009.05.009","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/19445949","host_type":"repository"}],"fields_of_study":["DNA Repair Mechanisms","DNA and Nucleic Acid Chemistry","Carcinogens and Genotoxicity Assessment","DNA","DNA Repair","DNA, Single-Stranded","Models, Biological","Protein Binding","Protein Interaction Mapping","Rad51 Recombinase","Rad52 DNA Repair and Recombination Protein","Recombination, Genetic","Replication Protein A","Saccharomyces cerevisiae","Saccharomyces cerevisiae Proteins"],"mesh_terms":["DNA","DNA Repair","DNA, Single-Stranded","Models, Biological","Protein Binding","Recombination, Genetic","Saccharomyces cerevisiae","Protein Interaction Mapping","Saccharomyces cerevisiae Proteins","Rad51 Recombinase","Replication Protein A","Rad52 DNA Repair and Recombination Protein"],"keywords":["RAD52","RAD51","Replication protein A","DNA repair","DNA","Biology","Homologous recombination","Cell biology","Chemistry","DNA-binding protein","Biochemistry","Transcription factor","Gene"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-02T18:15:09.862486Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}