ArticleNucleic acids research2017
Bacillus subtilis RecA with DprA-SsbA antagonizes RecX function during natural transformation.
Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 36 citations in OpenAlex.
- Mechanistic insights into the structure and function of the RecA C-terminal tail.Communications biology · 2026Article
- Nucleoid structure and dynamics influence natural chromosomal transformation in Bacillus subtilis: the role of EbfC.Nucleic acids research · 2025Article
- A Single DNA Binding Site of DprA Dimer Is Required to Facilitate RecA Filament Nucleation.International journal of molecular sciences · 2025Article
- Hallmarks of DNA replication stress responses in Escherichia coli and Bacillus subtilis.FEMS microbiology reviews · 2025Review
- Molecular mechanisms and applications of natural transformation in bacteria.Frontiers in microbiology · 2025Review
- Genomic signatures of cold adaptation in the family Colwelliaceae.Extremophiles : life under extreme conditions · 2024Article
- Processing of stalled replication forks in Bacillus subtilis.FEMS microbiology reviews · 2024Review
- Article
- Genomic Insights into the Radiation-Resistant Capability ofMicroorganisms · 2022Article
- A new insight into RecA filament regulation by RecX from the analysis of conformation-specific interactions.eLife · 2022Article
- The RecD2 helicase balances RecA activities.Nucleic acids research · 2022Article
- PcrA Dissociates RecA Filaments and the SsbA and RecO Mediators Counterbalance Such Activity.Frontiers in molecular biosciences · 2022Article
- Effect of Nutritional Determinants and TonB on the Natural Transformation ofFrontiers in microbiology · 2021Article
- Modulating mechanical stability of heterodimerization between engineered orthogonal helical domains.Nature communications · 2020Article
- Article
- Article
- Bacillus subtilis RecA interacts with and loads RadA/Sms to unwind recombination intermediates during natural chromosomal transformation.Nucleic acids research · 2019Article
- Single molecule tracking reveals functions for RarA at replication forks but also independently from replication during DNA repair in Bacillus subtilis.Scientific reports · 2019Article
- Article
- Pull in and Push Out: Mechanisms of Horizontal Gene Transfer in Bacteria.Frontiers in microbiology · 2018Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacillus subtilis DprA and RecX proteins, which interact with RecA, are crucial for efficient chromosomal and plasmid transformation. We showed that RecA, in the rATP·Mg2+ bound form (RecA·ATP), could not compete with RecX, SsbA or SsbB for assembly onto single-stranded (ss)DNA, but RecA·dATP partially displaced these proteins from ssDNA. RecX promoted reversible depolymerization of preformed RecA·ATP filaments. The two-component DprA-SsbA mediator reversed the RecX negative effect on RecA filament extension, but not DprA or DprA and SsbB. In the presence of DprA-SsbA, RecX added prior to RecA·ATP inhibited DNA strand exchange, but this inhibition was reversed when RecX was added after RecA. We propose that RecA nucleation is more sensitive to RecX action than is RecA filament growth. DprA-SsbA facilitates formation of an active RecA filament that directly antagonizes the inhibitory effects of RecX. RecX and DprA enable chromosomal transformation by altering RecA filament dynamics. DprA-SsbA and RecX proteins constitute a new regulatory network of RecA function. DprA-SsbA contributes to the formation of an active RecA filament and directly antagonizes the inhibitory effects of RecX during natural transformation.
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