ArticleScientific reports2017
Stable Nuclei of Nucleoprotein Filament and High ssDNA Binding Affinity Contribute to Enhanced RecA E38K Recombinase Activity.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 10 citations in OpenAlex.
- Nucleostemin promotes RAD51 filament assembly on double-stranded DNA to protect stalled replication forks.Nucleic acids research · 2026Article
- Single-molecule fluorescence reveals the DNA unwinding mechanism of mitochondrial helicase TWINKLE and its interplay with single-stranded DNA-binding proteins.Nucleic acids research · 2025Article
- NProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Nuclease-induced stepwise photodropping (NISP) to precisely investigate single-stranded DNA degradation behaviors of exonucleases and endonucleases.Nucleic acids research · 2024Article
- Hop2-Mnd1 and Swi5-Sfr1 stimulate Dmc1 filament assembly using distinct mechanisms.Nucleic acids research · 2023Article
- Positive Charges Are Important for the SOS Constitutive Phenotype inJournal of bacteriology · 2022Article
- The regulation mechanism of the C-terminus of RecA proteins during DNA strand-exchange process.Biophysical journal · 2021Article
- Single-Molecule Tethered Particle Motion Studies on the DNA Recombinase Filament Assembly and Disassembly.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Microcephaly family protein MCPH1 stabilizes RAD51 filaments.Nucleic acids research · 2020Article
- A Comprehensive View of Translesion Synthesis in Escherichia coli.Microbiology and molecular biology reviews : MMBR · 2020Review
- Swi5-Sfr1 stimulates Rad51 recombinase filament assembly by modulating Rad51 dissociation.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
RecA plays central roles in the homologous recombination to repair double-stranded DNA break damage in E. coli. A previously identified recA strain surviving high doses of UV radiation includes a dominant RecA E38K mutation. Using single-molecule experiments, we showed that the RecA E38K variant protein assembles nucleoprotein filaments more rapidly than the wild-type RecA. We also used a single-molecule fluorescence resonance energy transfer (smFRET) experiment to compare the nucleation cluster dynamics of wild-type RecA and RecA E38K mutants on various short ssDNA substrates. At shorter ssDNA, nucleation clusters of RecA E38K form dynamically, while only few were seen in wild-type RecA. RecA E38K also forms stable nuclei by specifically lowering the dissociation rate constant, k
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