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

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

Genes to cells : devoted to molecular & cellular mechanisms - 1 Sept 2003

Hishida Takashi, Iwasaki Hiroshi, Han Yong-Woon, Ohnishi Takayuki, Shinagawa Hideo

Abstract excerpt

BACKGROUND: Escherichia coli RuvAB promotes branch migration of Holliday junctions during recombination repair and homologous recombination. RuvB forms a hexameric ring through which duplex DNA passes and is translocated in an ATP-dependent manner. ATPase-deficient RuvB mutant K68A has a mutation...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Triphosphatases
Share to Bacterial Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to DNA-Binding Proteins

Share to DNA Helicases

Share to Escherichia coli Proteins

Share to Macromolecular Substances

Share to Rec A Recombinases

Share to Recombination, Genetic

Source

Identifiers

PMID: 12940820
DOI: 10.1046/j.1365-2443.2003.00670.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-12940820-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Uncoupling of the ATPase activity from the branch migration activity of RuvAB protein complexes containing both wild-type and ATPase-defective RuvB proteins.PMID 12940820Read ↗

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 ↗

Direct evidence that a conserved arginine in RuvB AAA+ ATPase acts as an allosteric effector for the ATPase activity of the adjacent subunit in a hexamer.Semantic proximity Read ↗

Helicase-defective RuvB(D113E) promotes RuvAB-mediated branch migration in vitro.Semantic proximity Read ↗

Structure and mechanism of the RuvB Holliday junction branch migration motor.Semantic proximity Read ↗

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 ↗

Structure-function analysis of the three domains of RuvB DNA motor protein.Semantic proximity Read ↗

ruvA Mutants that resolve Holliday junctions but do not reverse replication forks.Semantic proximity Read ↗

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

Modulation of RuvB function by the mobile domain III of the Holliday junction recognition protein RuvA.Semantic proximity Read ↗

The RuvABC resolvasome.Semantic proximity Read ↗

Molecular mechanisms of Holliday junction processing in Escherichia coli.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 ↗

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