{"doi":"10.1101/2022.12.05.519199","title":"Interaction with single-stranded DNA-binding protein modulates <i>Escherichia coli</i> RadD DNA repair activities","abstract":"Abstract The bacterial RadD enzyme is important for multiple genome maintenance pathways, including RecA DNA strand exchange and RecA-independent suppression of DNA crossover template switching. However, much remains unknown about the precise roles of RadD. One potential clue into RadD mechanisms is its direct interaction with the single-stranded DNA binding protein (SSB), which coats single-stranded DNA exposed during genome maintenance reactions in cells. Interaction with SSB stimulates the ATPase activity of RadD. To probe the mechanism and importance of RadD/SSB complex formation, we identified a pocket on RadD that is essential for binding SSB. In a mechanism shared with many other SSB-interacting proteins, RadD uses a hydrophobic pocket framed by basic residues to bind the C-terminal end of SSB. RadD variants that substitute acidic residues for basic residues in the SSB binding site impair RadD/SSB complex formation and eliminate SSB stimulation of RadD ATPase activity in vitro . Mutant E. coli strains carrying charge reversal radD changes display increased sensitivity to DNA damaging agents synergistically with deletions of radA and recG , although the phenotypes of the SSB-binding radD mutants are not as severe a full radD deletion. This suggests that RadD has multiple functions in the cell, with a subset requiring the interaction with SSB.","journal":"bioRxiv (Cold Spring Harbor Laboratory)","year":2022,"id":305042,"datarank":0.10397207708399181,"base_score":0.6931471805599453,"endowment":0.6931471805599453,"self_citation_contribution":0.10397207708399181,"citation_network_contribution":0.0,"self_endowment_contribution":0.10397207708399181,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":1,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":0.9537,"is_data_producer":false,"deposit_databanks":null,"is_oa":true,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":"2022-01-01","fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":406653,"name":"Elizabeth A. Wood","orcid":"0000-0002-7769-8481","position":1,"is_corresponding":false},{"id":475676,"name":"James L. Keck","orcid":"0000-0002-5961-0220","position":2,"is_corresponding":false},{"id":406656,"name":"Michael M. Cox","orcid":"0000-0003-3606-5722","position":3,"is_corresponding":false},{"id":998505,"name":"Miguel A. Osorio Garcia","orcid":"0000-0002-0984-837X","position":0,"is_corresponding":true}],"reference_count":58,"raw_metadata":{"citation_network_status":"fetched"},"created_at":"2026-07-19T00:32:37.185846Z","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":[]}