Direct rescue of stalled DNA replication forks via the combined action of PriA and RecG helicase activities

A. V. Gregg, Peter McGlynn, R. G. Lloyd, R. P. Jaktaji

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107 Citations (Scopus)

Abstract

The PriA protein of Escherichia coli plays a key role in the rescue of replication forks stalled on the template DNA. One attractive model of rescue relies on homologous recombination to establish a new fork via PriA-mediated loading of the DnaB replicative helicase at D loop intermediates. We provide genetic and biochemical evidence that PriA helicase activity can also rescue a stalled fork by an alternative mechanism that requires manipulation of the fork before loading of DnaB on the lagging strand template. This direct rescue depends on RecG, which unwinds forks and Holliday junctions and interconverts these structures. The combined action of PriA and RecG helicase activities may thus avoid the potential dangers of rescue pathways Involving fork breakage and recombination.

Original languageEnglish
Pages (from-to)241-251
Number of pages10
JournalMolecular Cell
Volume9
Issue number2
DOIs
Publication statusPublished - 2002

Keywords

  • ESCHERICHIA-COLI K-12
  • HOLLIDAY JUNCTIONS
  • PROTEIN PRIA
  • RECOMBINATION
  • MUTANTS
  • MUTATIONS
  • REPAIR
  • SUPPRESSION
  • STRAND
  • INTERMEDIATE

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