ArticleNucleic acids research2007
Real-time measurements of the nucleation, growth and dissociation of single Rad51-DNA nucleoprotein filaments.
Article in Nucleic acids research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 85 citations in OpenAlex.
- NProceedings of the National Academy of Sciences of the United States of America · 2025Article
- SWI5-SFR1 reduces RAD51 recombinase extending units during filament assembly.Nucleic acids research · 2025Article
- A large C-terminal Rad52 segment acts as a chaperone to Form and Stabilize Rad51 Filaments.Nature communications · 2025Article
- During recombinase-mediated homology recognition RecQ helicases inhibit formation of toxic long-lived D-loops that could promote genomic instability.Nucleic acids research · 2025Article
- Human RAD52 stimulates the RAD51-mediated homology search.Life science alliance · 2024Article
- Fibrillarin promotes homologous recombination repair by facilitating the recruitment of recombinase RAD51 to DNA damage sites.Journal of Zhejiang University. Science. B · 2023Article
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- The relationship between defects in DNA repair genes and autoinflammatory diseases.Rheumatology international · 2022Review
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- Single molecule microscopy reveals key physical features of repair foci in living cells.eLife · 2021Article
- Single Molecule Study of the Polymerization of RecA on dsDNA: The Dynamics of Individual Domains.Frontiers in molecular biosciences · 2021Article
- RAD51 discrimination between single- and double-strand DNA: a matter of flexibility and enthalpy.The EMBO journal · 2020Article
- Molecular flexibility of DNA as a key determinant of RAD51 recruitment.The EMBO journal · 2020Article
- Complex Chromatin Motions for DNA Repair.Frontiers in genetics · 2020Review
- RPA and RAD51: fork reversal, fork protection, and genome stability.Nature structural & molecular biology · 2018Review
- Single-molecule localization microscopy reveals molecular transactions during RAD51 filament assembly at cellular DNA damage sites.Nucleic acids research · 2018Article
- Multi-scale tracking reveals scale-dependent chromatin dynamics after DNA damage.Molecular biology of the cell · 2017Article
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Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human Rad51 (hRad51), the protein central to DNA pairing and strand exchange during homologous recombination, polymerizes on DNA to form nucleoprotein filaments. By making use of magnetic tweezers to manipulate individual DNA molecules, we measured the nucleation and growth of hRad51 nucleoprotein filaments, and their subsequent disassembly in real time. The dependence of the initial polymerization rate upon the concentration of hRad51 suggests that the rate-limiting step is the formation of a nucleus involving 5.5 +/- 1.5 hRad51 monomers, corresponding to one helical turn of the hRad51 nucleoprotein filament. Polymerization is highly cooperative (i.e. a nucleation-limited reaction) at low concentrations and less cooperative (a growth-limited reaction) at high concentrations of the protein. We show that the observed preference of hRad51 to form nucleoprotein filaments on double-stranded DNA rather than on single-stranded DNA is due to the fact that it depolymerizes much faster from ssDNA than from dsDNA: indeed, hRad51 polymerizes faster on ssDNA than on dsDNA. Hydrolysis of ATP by hRad51 does not correlate with its dissociation from dsDNA. This suggests that hRad51 does not depolymerize rapidly from dsDNA after strand exchange but stays bound to the heteroduplex, highlighting the importance of partner proteins to facilitate hRad51 depolymerization from dsDNA.
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