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

ruvA Mutants that resolve Holliday junctions but do not reverse replication forks.

PLoS genetics - 7 Mar 2008

Baharoglu Zeynep, Bradley Alison Sylvia, Le Masson Marie, Tsaneva Irina, Michel Bénédicte

Abstract excerpt

RuvAB and RuvABC complexes catalyze branch migration and resolution of Holliday junctions (HJs) respectively. In addition to their action in the last steps of homologous recombination, they process HJs made by replication fork reversal, a reaction which occurs at inactivated replication forks by the annealing of blocked leading and lagging strand ends. RuvAB was recently proposed to bind replication forks and...

Read the complete abstract on PubMed

Topics

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

Share to DNA Helicases
Share to DNA Repair
Share to DNA Replication

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Escherichia coli Proteins

Share to Genes, Bacterial

Share to Mutagenesis, Site-Directed

Share to Radiation Tolerance

Share to Recombination, Genetic

Source

Open in PubMed Open full text

Identifiers

PMID: 18369438
DOI: 10.1371/journal.pgen.1000012
PMCID: PMC2265524

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

ruvA Mutants that resolve Holliday junctions but do not reverse replication forks.PMID 18369438Read ↗

Formation of a stable RuvA protein double tetramer is required for efficient branch migration in vitro and for replication fork reversal in vivo.Semantic proximity Read ↗

RuvABC is required to resolve holliday junctions that accumulate following replication on damaged templates in Escherichia coli.Semantic proximity Read ↗

Mycobacterium tuberculosis RuvA induces two distinct types of structural distortions between the homologous and heterologous Holliday junctions.Semantic proximity Read ↗

RuvAB is essential for replication forks reversal in certain replication mutants.Semantic proximity Read ↗

Escherichia coli RuvBL268S: a mutant RuvB protein that exhibits wild-type activities in vitro but confers a UV-sensitive ruv phenotype in vivo.Semantic proximity Read ↗

Resolution of holliday junctions by RuvABC prevents dimer formation in rep mutants and UV-irradiated cells.Semantic proximity Read ↗

Uncoupling of the ATPase activity from the branch migration activity of RuvAB protein complexes containing both wild-type and ATPase-defective RuvB proteins.Semantic proximity Read ↗

RuvAB acts at arrested replication forks.Semantic proximity Read ↗

The RuvAB branch migration translocase and RecU Holliday junction resolvase are required for double-stranded DNA break repair in Bacillus subtilis.Semantic proximity Read ↗

The RuvABC resolvasome.Semantic proximity Read ↗

Abortive recombination in Escherichia coli ruv mutants blocks chromosome partitioning.Semantic proximity Read ↗

The RuvABC resolvase is indispensable for recombinational repair in sbcB15 mutants of Escherichia coli.Semantic proximity Read ↗

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