ArticleThe Journal of biological chemistry2015
Induction of Plasmid Conjugation in Bacillus subtilis Is Bistable and Driven by a Direct Interaction of a Rap/Phr Quorum-sensing System with a Master Repressor.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 12 citations in OpenAlex.
- A native conjugative plasmid confers potential selective advantages to plant growth-promoting Bacillus velezensis strain GH1-13.Communications biology · 2021Article
- Inactivation of the dimeric RappLS20 anti-repressor of the conjugation operon is mediated by peptide-induced tetramerization.Nucleic acids research · 2020Article
- Multiple and Overlapping Functions of Quorum Sensing Proteins for Cell Specialization inJournal of bacteriology · 2020Review
- Ratiometric population sensing by a pump-probe signaling system in Bacillus subtilis.Nature communications · 2020Article
- Surface Exclusion Revisited: Function Related to Differential Expression of the Surface Exclusion System ofFrontiers in microbiology · 2019Article
- Regulation of Gram-Positive Conjugation.Frontiers in microbiology · 2019Review
- Social behaviours by Bacillus subtilis: quorum sensing, kin discrimination and beyond.Molecular microbiology · 2018Review
- A novel method for transforming the thermophilic bacterium Geobacillus kaustophilus.Microbial cell factories · 2018Article
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Conjugation of plasmid pLS20 from Bacillus subtilis is limited to a time window between early and late exponential growth. Genetic evidence has suggested that pLS20-encoded protein RcoLS20 represses expression of a large conjugation operon, whereas Rap protein RapLS20 relieves repression. We show that RapLS20 is a true antirepressor protein that forms dimers in vivo and in vitro and that it directly binds to the repressor protein RcoLS20 in a 1:1 stoichiometry. We provide evidence that RapLS20 binds to the helix-turn-helix-containing domain of RcoLS20 in vivo, probably obstructing DNA binding of RcoLS20, as seen in competitive DNA binding experiments. The activity of RapLS20 in turn is counteracted by the addition of the cognate PhrLS20 peptide, which directly binds to the Rap protein and presumably induces a conformational change of the antirepressor. Thus, a Rap protein acts directly as an antirepressor protein during regulation of plasmid conjugation, turning on conjugation, and is counteracted by the PhrLS20 peptide, which, by analogy to known Rap/Phr systems, is secreted and taken back up into the cells, mediating cell density-driven regulation. Finally, we show that this switchlike process establishes a population heterogeneity, where up to 30% of the cells induce transcription of the conjugation operon.
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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.