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

Research output: Contribution to journalArticle

106 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

Cite this

Direct rescue of stalled DNA replication forks via the combined action of PriA and RecG helicase activities. / Gregg, A. V.; McGlynn, Peter; Lloyd, R. G.; Jaktaji, R. P.

In: Molecular Cell, Vol. 9, No. 2, 2002, p. 241-251.

Research output: Contribution to journalArticle

Gregg, A. V. ; McGlynn, Peter ; Lloyd, R. G. ; Jaktaji, R. P. / Direct rescue of stalled DNA replication forks via the combined action of PriA and RecG helicase activities. In: Molecular Cell. 2002 ; Vol. 9, No. 2. pp. 241-251.
@article{0564fd2ec10940418695412efba57fd0,
title = "Direct rescue of stalled DNA replication forks via the combined action of PriA and RecG helicase activities",
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.",
keywords = "ESCHERICHIA-COLI K-12, HOLLIDAY JUNCTIONS, PROTEIN PRIA, RECOMBINATION, MUTANTS, MUTATIONS, REPAIR, SUPPRESSION, STRAND, INTERMEDIATE",
author = "Gregg, {A. V.} and Peter McGlynn and Lloyd, {R. G.} and Jaktaji, {R. P.}",
year = "2002",
doi = "10.1016/S1097-2765(02)00455-0",
language = "English",
volume = "9",
pages = "241--251",
journal = "Molecular Cell",
issn = "1097-2765",
publisher = "Cell Press",
number = "2",

}

TY - JOUR

T1 - Direct rescue of stalled DNA replication forks via the combined action of PriA and RecG helicase activities

AU - Gregg, A. V.

AU - McGlynn, Peter

AU - Lloyd, R. G.

AU - Jaktaji, R. P.

PY - 2002

Y1 - 2002

N2 - 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.

AB - 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.

KW - ESCHERICHIA-COLI K-12

KW - HOLLIDAY JUNCTIONS

KW - PROTEIN PRIA

KW - RECOMBINATION

KW - MUTANTS

KW - MUTATIONS

KW - REPAIR

KW - SUPPRESSION

KW - STRAND

KW - INTERMEDIATE

U2 - 10.1016/S1097-2765(02)00455-0

DO - 10.1016/S1097-2765(02)00455-0

M3 - Article

VL - 9

SP - 241

EP - 251

JO - Molecular Cell

JF - Molecular Cell

SN - 1097-2765

IS - 2

ER -