The DNA replication priming protein, PriA, is required for homologous recombination and double-strand break repair.

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.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Kogoma T,Cadwell GW,Barnard KG,Asai T

doi

10.1128/jb.178.5.1258-1264.1996

subject

Has Abstract

pub_date

1996-03-01 00:00:00

pages

1258-64

issue

5

eissn

0021-9193

issn

1098-5530

journal_volume

178

pub_type

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