ArticleNucleic acids research2009
Dynamics of RecA filaments on single-stranded DNA.
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 52 papers.
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Who cites it
52 citing papers in PubMed.
- Antiphage defence systems Druantia III and Zorya II synergise via shared DNA intermediates in a phage-specific manner.bioRxiv : the preprint server for biology · 2026Article
- Structure, function, and applications of two novel phage recombinases from extreme environments.Nucleic acids research · 2026Article
- NProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structure of RADX and mechanism for regulation of RAD51 nucleofilaments.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Unravelling DNA Organization with Single-Molecule Force Spectroscopy Using Magnetic Tweezers.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Divalent metal cofactors differentially modulate RadA-mediated strand invasion and exchange in Saccharolobus solfataricus.Bioscience reports · 2023Article
- SMC protein RecN drives RecA filament translocation for in vivo homology search.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- A new insight into RecA filament regulation by RecX from the analysis of conformation-specific interactions.eLife · 2022Article
- Single-molecule fluorescence imaging techniques reveal molecular mechanisms underlying deoxyribonucleic acid damage repair.Frontiers in bioengineering and biotechnology · 2022Review
- How strand exchange protein function benefits from ATP hydrolysis.Current opinion in genetics & development · 2021Review
- The regulation mechanism of the C-terminus of RecA proteins during DNA strand-exchange process.Biophysical journal · 2021Article
- Single-molecule insight into stalled replication fork rescue in Escherichia coli.Nucleic acids research · 2021Review
- Micro-homology intermediates: RecA's transient sampling revealed at the single molecule level.Nucleic acids research · 2021Article
- PprA Protein Inhibits DNA Strand Exchange and ATP Hydrolysis ofFrontiers in cell and developmental biology · 2021Article
- Single Molecule Study of the Polymerization of RecA on dsDNA: The Dynamics of Individual Domains.Frontiers in molecular biosciences · 2021Article
- Single-Molecule Insights into ATP-Dependent Conformational Dynamics of Nucleoprotein Filaments ofInternational journal of molecular sciences · 2020Article
- A Comprehensive View of Translesion Synthesis in Escherichia coli.Microbiology and molecular biology reviews : MMBR · 2020Review
- Modular microfluidics enables kinetic insight from time-resolved cryo-EM.Nature communications · 2020Article
- Weaving DNA strands: structural insight on ATP hydrolysis in RecA-induced homologous recombination.Nucleic acids research · 2019Article
- In vivo genome editing rescues photoreceptor degeneration via a Cas9/RecA-mediated homology-directed repair pathway.Science advances · 2019Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
RecA, the key protein in homologous recombination, performs its actions as a helical filament on single-stranded DNA (ssDNA). ATP hydrolysis makes the RecA-ssDNA filament dynamic and is essential for successful recombination. RecA has been studied extensively by single-molecule techniques on double-stranded DNA (dsDNA). Here we directly probe the structure and kinetics of RecA interaction with its biologically most relevant substrate, long ssDNA molecules. We find that RecA ATPase activity is required for the formation of long continuous filaments on ssDNA. These filaments both nucleate and extend with a multimeric unit as indicated by the Hill coefficient of 5.4 for filament nucleation. Disassembly rates of RecA from ssDNA decrease with applied stretching force, corresponding to a mechanism where protein-induced stretching of the ssDNA aids in the disassembly. Finally, we show that RecA-ssDNA filaments can reversibly interconvert between an extended, ATP-bound, and a compressed, ADP-bound state. Taken together, our results demonstrate that ATP hydrolysis has a major influence on the structure and state of RecA filaments on ssDNA.
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