ArticleThe Journal of biological chemistry2012
RAD51 protein ATP cap regulates nucleoprotein filament stability.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
23 citing papers in PubMed, 31 citations in OpenAlex.
- Cancer mutations in RAD51 and its paralogues.PloS one · 2026Article
- In silico structural analysis of Oryza sativa RAD51 reveals key interactions for nucleoprotein filament assembly and regulation.PloS one · 2025Article
- The Swi5-Sfr1 complex regulates Dmc1- and Rad51-driven DNA strand exchange proceeding through two distinct three-stranded intermediates by different mechanisms.Nucleic acids research · 2024Article
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- Article
- Divalent metal cofactors differentially modulate RadA-mediated strand invasion and exchange in Saccharolobus solfataricus.Bioscience reports · 2023Article
- Mechanisms of distinctive mismatch tolerance between Rad51 and Dmc1 in homologous recombination.Nucleic acids research · 2021Article
- Nucleotide proofreading functions by nematode RAD51 paralogs facilitate optimal RAD51 filament function.Nature communications · 2021Article
- Rrp1 translocase and ubiquitin ligase activities restrict the genome destabilising effects of Rad51 in fission yeast.Nucleic acids research · 2021Article
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- Dynamic unwrapping of nucleosomes by HsRAD51 that includes sliding and rotational motion of histone octamers.Nucleic acids research · 2017Article
- Cryo-EM structures of human RAD51 recombinase filaments during catalysis of DNA-strand exchange.Nature structural & molecular biology · 2017Article
- Tyrosine phosphorylation stimulates activity of human RAD51 recombinase through altered nucleoprotein filament dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Dynamic binding of replication protein a is required for DNA repair.Nucleic acids research · 2016Article
- Dynamic control of strand excision during human DNA mismatch repair.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Functional Relationship of ATP Hydrolysis, Presynaptic Filament Stability, and Homologous DNA Pairing Activity of the Human Meiotic Recombinase DMC1.The Journal of biological chemistry · 2015Article
- TRF1 and TRF2 differentially modulate Rad51-mediated telomeric and nontelomeric displacement loop formation in vitro.Biochemistry · 2014Article
- Strand invasion by HLTF as a mechanism for template switch in fork rescue.Nucleic acids research · 2014Article
- Mismatch repair protein hMSH2-hMSH6 recognizes mismatches and forms sliding clamps within a D-loop recombination intermediate.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- The HsRAD51B-HsRAD51C stabilizes the HsRAD51 nucleoprotein filament.DNA repair · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 6 institutions in 2 countries.
Funding
Abstract
RAD51 mediates homologous recombination by forming an active DNA nucleoprotein filament (NPF). A conserved aspartate that forms a salt bridge with the ATP γ-phosphate is found at the nucleotide-binding interface between RAD51 subunits of the NPF known as the ATP cap. The salt bridge accounts for the nonphysiological cation(s) required to fully activate the RAD51 NPF. In contrast, RecA homologs and most RAD51 paralogs contain a conserved lysine at the analogous structural position. We demonstrate that substitution of human RAD51(Asp-316) with lysine (HsRAD51(D316K)) decreases NPF turnover and facilitates considerably improved recombinase functions. Structural analysis shows that archaebacterial Methanococcus voltae RadA(D302K) (MvRAD51(D302K)) and HsRAD51(D316K) form extended active NPFs without salt. These studies suggest that the HsRAD51(Asp-316) salt bridge may function as a conformational sensor that enhances turnover at the expense of recombinase activity.
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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.