ArticleNucleic acids research2018
The ATPase activity of E. coli RecA prevents accumulation of toxic complexes formed by erroneous binding to undamaged double stranded DNA.
Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 30 citations in OpenAlex.
- Structure, function, and applications of two novel phage recombinases from extreme environments.Nucleic acids research · 2026Article
- Mei5-Sae3 stabilizes both active and inactive forms of Dmc1 filaments independently of its impact on ATP hydrolysis.Nucleic acids research · 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
- Binding Behavior of Human Hepatoma-Derived Growth Factor onThe journal of physical chemistry. B · 2024Article
- Computational Insights into the Dynamic Structural Features and Binding Characteristics of Recombinase UvsX Compared with RecA.Molecules (Basel, Switzerland) · 2023Article
- Divalent metal cofactors differentially modulate RadA-mediated strand invasion and exchange in Saccharolobus solfataricus.Bioscience reports · 2023Article
- ATPase Activity of Bacillus subtilis RecA Affects the Dynamic Formation of RecA Filaments at DNA Double Strand Breaks.mSphere · 2022Article
- How strand exchange protein function benefits from ATP hydrolysis.Current opinion in genetics & development · 2021Review
- Article
- Biological characteristics and genomic analysis of a Stenotrophomonas maltophilia phage vB_SmaS_BUCT548.Virus genes · 2021Article
- Single-molecule analysis reveals cooperative stimulation of Rad51 filament nucleation and growth by mediator proteins.Molecular cell · 2021Article
- Precise sequencing of single protected-DNA fragment molecules for profiling of protein distribution and assembly on DNA.Chemical science · 2021Article
- A mutant form of Dmc1 that bypasses the requirement for accessory protein Mei5-Sae3 reveals independent activities of Mei5-Sae3 and Rad51 in Dmc1 filament stability.PLoS genetics · 2019Article
- Omnipresent Maxwell's demons orchestrate information management in living cells.Microbial biotechnology · 2019Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The Escherichia coli RecA protein catalyzes the central step of homologous recombination using its homology search and strand exchange activity. RecA is a DNA-dependent ATPase, but its homology search and strand exchange activities are largely independent of its ATPase activity. ATP hydrolysis converts a high affinity DNA binding form, RecA-ATP, to a low affinity form RecA-ADP, thereby supporting an ATP hydrolysis-dependent dynamic cycle of DNA binding and dissociation. We provide evidence for a novel function of RecA's dynamic behavior; RecA's ATPase activity prevents accumulation of toxic complexes caused by direct binding of RecA to undamaged regions of dsDNA. We show that a mutant form of RecA, RecA-K250N, previously shown to be toxic to E. coli, is a loss-of-function ATPase-defective mutant. We use a new method for detecting RecA complexes involving nucleoid surface spreading and immunostaining. The method allows detection of damage-induced RecA foci; STED microscopy revealed these to typically be between 50 and 200 nm in length. RecA-K250N, and other toxic variants of RecA, form spontaneous DNA-bound complexes that are independent of replication and of accessory proteins required to load RecA onto tracts of ssDNA in vivo, supporting the hypothesis that RecA's expenditure of ATP serves an error correction function.
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