Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

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

Molecular cell - 1 Feb 2002

Gregg Amanda V, McGlynn Peter, Jaktaji Razieh P, Lloyd Robert G

Abstract excerpt

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...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Nucleic Acid Conformation
Share to Adenosine Triphosphatases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to DNA Helicases

Share to DNA Replication

Share to Endodeoxyribonucleases

Share to Macromolecular Substances

Share to Templates, Genetic

Share to Ultraviolet Rays

Source

Identifiers

PMID: 11864599
DOI: 10.1016/s1097-2765(02)00455-0

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Direct rescue of stalled DNA replication forks via the combined action of PriA and RecG helicase activities.PMID 11864599Read ↗

Stabilization of a stalled replication fork by concerted actions of two helicases.Semantic proximity Read ↗

RecG Directs DNA Synthesis during Double-Strand Break Repair.Semantic proximity Read ↗

PriA-directed replication fork restart in Escherichia coli.Semantic proximity Read ↗

Modulation of DNA damage tolerance in Escherichia coli recG and ruv strains by mutations affecting PriB, the ribosome and RNA polymerase.Semantic proximity Read ↗

Cells defective for replication restart undergo replication fork reversal.Semantic proximity Read ↗

RecG helicase promotes DNA double-strand break repair.Semantic proximity Read ↗

The RdgC protein of Escherichia coli binds DNA and counters a toxic effect of RecFOR in strains lacking the replication restart protein PriA.Semantic proximity Read ↗

Escherichia coli K-12 has two distinguishable PriA-PriB replication restart pathways.Semantic proximity Read ↗

Modulation of recombination and DNA repair by the RecG and PriA helicases of Escherichia coli K-12.Semantic proximity Read ↗

Requirement for RecFOR-mediated recombination in priA mutant.Semantic proximity Read ↗

Multiple genetic pathways for restarting DNA replication forks in Escherichia coli K-12.Semantic proximity Read ↗

Resolving Toxic DNA repair intermediates in every E. coli replication cycle: critical roles for RecG, Uup and RadD.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.