ArticleNucleic acids research2010
Insights into the mechanism of Rad51 recombinase from the structure and properties of a filament interface mutant.
Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 35 citations in OpenAlex.
- Structure, function, and applications of two novel phage recombinases from extreme environments.Nucleic acids research · 2026Article
- The bacteriophage T4 homologous recombination system: mechanism, applications, conservation, and environmental significance.EcoSal Plus · 2025Review
- Local structural dynamics of Rad51 protomers revealed by cryo-electron microscopy of Rad51-ssDNA filaments.Nucleic acids research · 2025Article
- CRISPR/Cas9‑induced saturated mutagenesis identifiesMolecular medicine reports · 2022Article
- A novel motif of Rad51 serves as an interaction hub for recombination auxiliary factors.eLife · 2021Article
- A small-molecule inhibitor of the DNA recombinase Rad51 fromThe Journal of biological chemistry · 2019Article
- Knockout of Babesia bovis rad51 ortholog and its complementation by expression from the BbACc3 artificial chromosome platform.PloS one · 2019Article
- Variation in RAD51 details a hub of functions: opportunities to advance cancer diagnosis and therapy.F1000Research · 2018Review
- Defects in recombination activity caused by somatic and germline mutations in the multimerization/BRCA2 binding region of human RAD51 protein.DNA repair · 2017Article
- A cell-penetrating antibody inhibits human RAD51 via direct binding.Nucleic acids research · 2017Article
- RAD51 variant proteins from human lung and kidney tumors exhibit DNA strand exchange defects.DNA repair · 2016Article
- ATP half-sites in RadA and RAD51 recombinases bind nucleotides.FEBS open bio · 2016Article
- DNA-pairing and annealing processes in homologous recombination and homology-directed repair.Cold Spring Harbor perspectives in biology · 2015Review
- Tumor-associated mutations in a conserved structural motif alter physical and biochemical properties of human RAD51 recombinase.Nucleic acids research · 2015Article
- DNA repair pathways in trypanosomatids: from DNA repair to drug resistance.Microbiology and molecular biology reviews : MMBR · 2014Review
- Molecular modeling and molecular dynamics simulations of recombinase Rad51.Biophysical journal · 2013Article
- Oxidative stress in mammalian cells impinges on the cysteines redox state of human XRCC3 protein and on its cellular localization.PloS one · 2013Article
- Probing Rad51-DNA interactions by changing DNA twist.Nucleic acids research · 2012Article
- Fission yeast Swi5-Sfr1 protein complex, an activator of Rad51 recombinase, forms an extremely elongated dogleg-shaped structure.The Journal of biological chemistry · 2011Article
- Presynaptic filament dynamics in homologous recombination and DNA repair.Critical reviews in biochemistry and molecular biology · 2011Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Rad51 protein promotes homologous recombination in eukaryotes. Recombination activities are activated by Rad51 filament assembly on ssDNA. Previous studies of yeast Rad51 showed that His352 occupies an important position at the filament interface, where it could relay signals between subunits and active sites. To investigate, we characterized yeast Rad51 H352A and H352Y mutants, and solved the structure of H352Y. H352A forms catalytically competent but salt-labile complexes on ssDNA. In contrast, H352Y forms salt-resistant complexes on ssDNA, but is defective in nucleotide exchange, RPA displacement and strand exchange with full-length DNA substrates. The 2.5 A crystal structure of H352Y reveals a right-handed helical filament in a high-pitch (130 A) conformation with P6(1) symmetry. The catalytic core and dimer interface regions of H352Y closely resemble those of DNA-bound Escherichia coli RecA protein. The H352Y mutation stabilizes Phe187 from the adjacent subunit in a position that interferes with the gamma-phosphate-binding site of the Walker A motif/P-loop, potentially explaining the limited catalysis observed. Comparison of Rad51 H352Y, RecA-DNA and related structures reveals that the presence of bound DNA correlates with the isomerization of a conserved cis peptide near Walker B to the trans configuration, which appears to prime the catalytic glutamate residue for ATP hydrolysis.
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