ArticleThe Journal of biological chemistry2013
Bacillus subtilis DprA recruits RecA onto single-stranded DNA and mediates annealing of complementary strands coated by SsbB and SsbA.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 72 citations in OpenAlex.
- Utilizing natural competence to genetically manipulateApplied and environmental microbiology · 2026Article
- Nucleoid structure and dynamics influence natural chromosomal transformation in Bacillus subtilis: the role of EbfC.Nucleic acids research · 2025Article
- Molecular interplay between ComEC domains allows for selective degradation of the non-translocating strand during natural transformation.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
- A conserved nuclease facilitates environmental DNA uptake.Nucleic acids research · 2025Article
- DprA recruits ComM to facilitate recombination during natural transformation in Gram-negative bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Naturally competent bacteria and their genetic parasites-a battle for control over horizontal gene transfer?FEMS microbiology reviews · 2025Review
- 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
- Visualizing dynamic competence pili and DNA capture throughout the long axis ofJournal of bacteriology · 2023Article
- Giving a signal: how protein phosphorylation helps Bacillus navigate through different life stages.FEMS microbiology reviews · 2023Review
- Visualizing dynamic competence pili and DNA capture throughout the long axis ofbioRxiv : the preprint server for biology · 2023Article
- CeONanomaterials (Basel, Switzerland) · 2023Article
- The RecA-directed recombination pathway of natural transformation initiates at chromosomal replication forks in the pneumococcus.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Single-Molecule Dynamics of DNA Receptor ComEA, Membrane Permease ComEC, and Taken-Up DNA in Competent Bacillus subtilis Cells.Journal of bacteriology · 2022Article
- Characterization of the DdrD protein from the extremely radioresistant bacterium Deinococcus radiodurans.Extremophiles : life under extreme conditions · 2021Article
- Natural Transformation inFrontiers in microbiology · 2020Article
- Bacillus subtilis RecA interacts with and loads RadA/Sms to unwind recombination intermediates during natural chromosomal transformation.Nucleic acids research · 2019Article
- Measurement of the Length of the Integrated Donor DNA duringBio-protocol · 2019Article
- Bacillus subtilis DisA regulates RecA-mediated DNA strand exchange.Nucleic acids research · 2019Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Naturally transformable bacteria recombine internalized ssDNA with a homologous resident duplex (chromosomal transformation) or complementary internalized ssDNAs (plasmid or viral transformation). Bacillus subtilis competence-induced DprA, RecA, SsbB, and SsbA proteins are involved in the early processing of the internalized ssDNA, with DprA physically interacting with RecA. SsbB and SsbA bind and melt secondary structures in ssDNA but limit RecA loading onto ssDNA. DprA binds to ssDNA and facilitates partial dislodging of both single-stranded binding (SSB) proteins from ssDNA. In the absence of homologous duplex DNA, DprA does not significantly increase RecA nucleation onto protein-free ssDNA. DprA facilitates RecA nucleation and filament extension onto SsbB-coated or SsbB plus SsbA-coated ssDNA. DprA facilitates RecA-mediated DNA strand exchange in the presence of both SSB proteins. DprA, which plays a crucial role in plasmid transformation, anneals complementary strands preferentially coated by SsbB to form duplex circular plasmid molecules. Our results provide a mechanistic framework for conceptualizing the coordinated events modulated by SsbB in concert with SsbA and DprA that are crucial for RecA-dependent chromosomal transformation and RecA-independent plasmid transformation.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.