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

Srs2 disassembles Rad51 filaments by a protein-protein interaction triggering ATP turnover and dissociation of Rad51 from DNA.

Molecular cell - 10 Jul 2009

Antony Edwin, Tomko Eric J, Xiao Qi, Krejci Lumir, Lohman Timothy M, Ellenberger Tom

Abstract excerpt

Rad51 is a DNA recombinase functioning in the repair of DNA double-strand breaks and the generation of genetic diversity by homologous recombination (HR). In the presence of ATP, Rad51 self-assembles into an extended polymer on single-stranded DNA to catalyze strand exchange. Inappropriate HR causes genomic instability, and it is normally prevented by remodeling enzymes that antagonize the activities of Rad51...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Triphosphate
Share to Carbocyanines

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to DNA Helicases

Share to DNA, Single-Stranded

Share to Fluorescence

Share to Hydrolysis

Share to Oligonucleotides

Share to Rad51 Recombinase

Source

Open in PubMed Open full text

Identifiers

PMID: 19595720
DOI: 10.1016/j.molcel.2009.05.026
PMCID: PMC2711036

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

Srs2 disassembles Rad51 filaments by a protein-protein interaction triggering ATP turnover and dissociation of Rad51 from DNA.PMID 19595720Read ↗

Remodeling of the Rad51 DNA strand-exchange protein by the Srs2 helicase.Semantic proximity Read ↗

Rad52 Oligomeric N-Terminal Domain Stabilizes Rad51 Nucleoprotein Filaments and Contributes to Their Protection against Srs2.Semantic proximity Read ↗

Dissociation of Rad51 Presynaptic Complexes and Heteroduplex DNA Joints by Tandem Assemblies of Srs2.Semantic proximity Read ↗

Role of ATP hydrolysis in the antirecombinase function of Saccharomyces cerevisiae Srs2 protein.Semantic proximity Read ↗

Rad52-Rad51 association is essential to protect Rad51 filaments against Srs2, but facultative for filament formation.Semantic proximity Read ↗

The Rad51 paralog complex Rad55-Rad57 acts as a molecular chaperone during homologous recombination.Semantic proximity Read ↗

Rad51 paralog complex Rad55–Rad57 acts as a molecular chaperone during homologous recombinationSemantic proximity Read ↗

Cdk1 targets Srs2 to complete synthesis-dependent strand annealing and to promote recombinational repair.Semantic proximity Read ↗

Srs2 and Mus81-Mms4 Prevent Accumulation of Toxic Inter-Homolog Recombination Intermediates.Semantic proximity Read ↗

The rad51-K191R ATPase-defective mutant is impaired for presynaptic filament formation.Semantic proximity Read ↗

Rad51 gain-of-function mutants that exhibit high affinity DNA binding cause DNA damage sensitivity in the absence of Srs2.Semantic proximity Read ↗

Insights into the mechanism of Rad51 recombinase from the structure and properties of a filament interface mutant.Semantic proximity Read ↗

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