ArticleNucleic acids research2009
Inter-subunit interactions that coordinate Rad51's activities.
Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
12 citing papers in PubMed, 19 citations in OpenAlex.
- Pathogenic variants in the human TONSL protein associated with SPONASTRIME dysplasia impair protein dimerization and DNA repair.Science advances · 2026Article
- The bacteriophage T4 homologous recombination system: mechanism, applications, conservation, and environmental significance.EcoSal Plus · 2025Review
- ATP hydrolysis-driven structural transitions within the Saccharomyces cerevisiae Rad51 and Dmc1 nucleoprotein filaments.The Journal of biological chemistry · 2025Article
- ATP hydrolysis-driven structural transitions within thebioRxiv : the preprint server for biology · 2025Article
- Local structural dynamics of Rad51 protomers revealed by cryo-electron microscopy of Rad51-ssDNA filaments.Nucleic acids research · 2025Article
- ATP half-sites in RadA and RAD51 recombinases bind nucleotides.FEBS open bio · 2016Article
- A novel Fanconi anaemia subtype associated with a dominant-negative mutation in RAD51.Nature communications · 2015Article
- Probing Rad51-DNA interactions by changing DNA twist.Nucleic acids research · 2012Article
- Regulation of Rad51 function by phosphorylation.EMBO reports · 2011Article
- Presynaptic filament dynamics in homologous recombination and DNA repair.Critical reviews in biochemistry and molecular biology · 2011Article
- Subunit interface residues F129 and H294 of human RAD51 are essential for recombinase function.PloS one · 2011Article
- Insights into the mechanism of Rad51 recombinase from the structure and properties of a filament interface mutant.Nucleic acids research · 2010Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Rad51 is the central catalyst of homologous recombination in eukaryotes and is thus critical for maintaining genomic integrity. Recent crystal structures of filaments formed by Rad51 and the closely related archeal RadA and eubacterial RecA proteins place the ATPase site at the protomeric interface. To test the relevance of this feature, we mutated conserved residues at this interface and examined their effects on key activities of Rad51: ssDNA-stimulated ATP hydrolysis, DNA binding, polymerization on DNA substrates and catalysis of strand-exchange reactions. Our results show that the interface seen in the crystal structures is very important for nucleoprotein filament formation. H352 and R357 of yeast Rad51 are essential for assembling the catalytically competent form of the enzyme on DNA substrates and coordinating its activities. However, contrary to some previous suggestions, neither of these residues is critical for ATP hydrolysis.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.