RRC ID 30139
Author Kogoma T, Cadwell GW, Barnard KG, Asai T.
Title The DNA replication priming protein, PriA, is required for homologous recombination and double-strand break repair.
Journal J. Bacteriol.
Abstract The PriA protein, a component of the phiX174-type primosome, was previously shown to be essential for damage-inducible DNA replication in Escherichia coli, termed inducible stable DNA replication. Here, we show that priA::kan null mutants are defective in transductional and conjugational homologous recombination and are hypersensitive to mitomycin C and gamma rays, which cause double-strand breaks. The introduction of a plasmid carrying the priA300 allele, which encodes a mutant PriA protein capable of catalyzing the assembly of an active primosome but which is missing the n'-pas-dependent ATPase, helicase, and translocase activities associated with PriA, alleviates the defects of priA::kan mutants in homologous recombination, double-strand break repair, and inducible stable DNA replication. Furthermore, spa-47, which was isolated as a suppressor of the broth sensitivity of priA::kan mutants, suppresses the Rec- and mitomycin C sensitivity phenotypes of priA::kan mutants. The spa-47 suppressor mutation maps within or very near dnaC. These results suggest that PriA-dependent primosome assembly is crucial for both homologous recombination and double-strand break repair and support the proposal that these processes in E. coli involve extensive DNA replication.
Volume 178(5)
Pages 1258-64
Published 1996-3
PMID 8631700
PMC PMC177797
MeSH Bacterial Proteins / metabolism DNA Damage DNA Repair* DNA Replication* DNA-Binding Proteins / genetics* DNA-Binding Proteins / metabolism Dose-Response Relationship, Radiation Escherichia coli / genetics* Escherichia coli Proteins* Exodeoxyribonucleases / metabolism Mutation Recombination, Genetic* Replication Protein A Suppression, Genetic Ultraviolet Rays / adverse effects
IF 3.234
Times Cited 140
Prokaryotes E. coli ME9579 ME9422 ME9376 ME9590 ME9591 ME9561 ME9530 ME9593