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J. Bacteriol., 12 1996, 6782-6789, Vol 178, No. 23
AA Al-Deib, AA Mahdi and RG Lloyd
The RecG protein of Escherichia coli is a structure-specific DNA helicase
that targets strand exchange intermediates in genetic recombination and
drives their branch migration along the DNA. Strains carrying null
mutations in recG show reduced recombination and DNA repair. Suppressors of
this phenotype, called srgA, were located close to metB and shown to be
alleles of priA. Suppression depends on the RecA, RecBCD, RecF, RuvAB, and
RuvC recombination proteins. Nine srgA mutations were sequenced and shown
to specify mutant PriA proteins with single amino acid substitutions
located in or close to one of the conserved helicase motifs. The mutant
proteins retain the ability to catalyze primosome assembly, as judged by
the viability of recG srgA and srgA strains and their ability to support
replication of plasmids based on the ColE1 replicon. Multicopy priA+
plasmids increase substantially the recombination- and repair-deficient
phenotype of recG strains and confer similar phenotypes on recG srgA double
mutants but not on ruvAB or wild-type strains. The multicopy effect is
eliminated by K230R, C446G, and C477G substitutions in PriA. It is
concluded that the 3'-5' DNA helicase/translocase activity of PriA inhibits
recombination and that this effect is normally countered by RecG.
Copyright © 1996, American Society for Microbiology
Modulation of recombination and DNA repair by the RecG and PriA helicases of Escherichia coli K-12
Department of Genetics, University of Nottingham, Queens Medical Centre, United Kingdom.
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