ArticleNucleic acids research2011
Single-molecule studies of the stringency factors and rates governing the polymerization of RecA on double-stranded DNA.
Article in Nucleic acids research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 12 citations in OpenAlex.
- Different relative scalings between transient forces and thermal fluctuations tune regimes of dynamic clustering.Physical review. E · 2025Article
- Single-molecule insight into stalled replication fork rescue in Escherichia coli.Nucleic acids research · 2021Review
- The poor homology stringency in the heteroduplex allows strand exchange to incorporate desirable mismatches without sacrificing recognition in vivo.Nucleic acids research · 2015Article
- Article
- The differential extension in dsDNA bound to Rad51 filaments may play important roles in homology recognition and strand exchange.Nucleic acids research · 2014Article
- Dynamics and Regulation of RecA Polymerization and De-Polymerization on Double-Stranded DNA.PloS one · 2013Article
- Kinetic mechanism for viral dsRNA length discrimination by MDA5 filaments.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Complementary strand relocation may play vital roles in RecA-based homology recognition.Nucleic acids research · 2012Article
- RecA homology search is promoted by mechanical stress along the scanned duplex DNA.Nucleic acids research · 2012Article
- Changes in the tension in dsDNA alter the conformation of RecA bound to dsDNA-RecA filaments.Nucleic acids research · 2011Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
RecA is a key protein in homologous recombination. During recombination, one single-stranded DNA (ssDNA) bound to site I in RecA exchanges Watson-Crick pairing with a sequence-matched ssDNA that was part of a double-stranded DNA molecule (dsDNA) bound to site II in RecA. After strand exchange, heteroduplex dsDNA is bound to site I. In vivo, direct polymerization of RecA on dsDNA through site I does not occur, though it does in vitro. The mechanisms underlying the difference have been unclear. We use single-molecule experiments to decouple the two steps involved in polymerization: nucleation and elongation. We find that elongation is governed by a fundamental clock that is insensitive to force and RecA concentration from 0.2 and 6 µM, though rates depend on ionic conditions. Thus, we can probe nucleation site stability by creating nucleation sites at high force and then measuring elongation as a function of applied force. We find that in the presence of ATP hydrolysis a minimum force is required for polymerization. The minimum force decreases with increasing RecA or ATP concentrations. We propose that force reduces the off-rate for nucleation site binding and that nucleation site stability is the stringency factor that prevents in vivo polymerization.
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Registered trials
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