ArticleToxins2016
Characterization of the Deep-Sea Streptomyces sp. SCSIO 02999 Derived VapC/VapB Toxin-Antitoxin System in Escherichia coli.
Article in Toxins, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 17 citations in OpenAlex.
- Warm-Water Regimes Influence Microbial Diversity and Ecological Functions in Subtropical Gulf.Ecology and evolution · 2026Article
- The Prevalence and Diversity of Marine Toxin-Antitoxin Systems.Marine drugs · 2025Article
- Evidence for a Functional HipBA Toxin-Antitoxin System inInternational journal of molecular sciences · 2025Article
- Type II Toxin-Antitoxin Systems inInfection and drug resistance · 2025Review
- Role of VapBC4 toxin-antitoxin system ofmBio · 2024Article
- The biological function of the type II toxin-antitoxin systemFrontiers in microbiology · 2024Article
- Toxin-antitoxin system gene mutations drivingFrontiers in microbiology · 2024Article
- Bacterial Toxin-Antitoxin Systems' Cross-Interactions-Implications for Practical Use in Medicine and Biotechnology.Toxins · 2023Review
- Applications of toxin-antitoxin systems in synthetic biology.Engineering microbiology · 2023Review
- Characterization and comparative analysis of toxin-antitoxin systems in Acetobacter pasteurianus.Journal of industrial microbiology & biotechnology · 2019Article
- Characterization of Two Toxin-Antitoxin Systems in Deep-SeaMarine drugs · 2019Article
- Article
- MqsR/MqsA Toxin/Antitoxin System Regulates Persistence and Biofilm Formation inFrontiers in microbiology · 2017Article
Corrections and comments
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Authors and funding
5 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Toxin-antitoxin (TA) systems are small genetic elements that are ubiquitous in prokaryotes. Most studies on TA systems have focused on commensal and pathogenic bacteria; yet very few studies have focused on TAs in marine bacteria, especially those isolated from a deep sea environment. Here, we characterized a type II VapC/VapB TA system from the deep-sea derived Streptomyces sp. SCSIO 02999. The VapC (virulence-associated protein) protein belongs to the PIN (PilT N-terminal) superfamily. Overproduction of VapC strongly inhibited cell growth and resulted in a bleb-containing morphology in E. coli. The toxicity of VapC was neutralized through direct protein-protein interaction by a small protein antitoxin VapB encoded by a neighboring gene. Antitoxin VapB alone or the VapB/VapC complex negatively regulated the vapBC promoter activity. We further revealed that three conserved Asp residues in the PIN domain were essential for the toxic effect of VapC. Additionally, the VapC/VapB TA system stabilized plasmid in E. coli. Furthermore, VapC cross-activated transcription of several TA operons via a partially Lon-dependent mechanism in E. coli, and the activated toxins accumulated more preferentially than their antitoxin partners. Collectively, we identified and characterized a new deep sea TA system in the deep sea Streptomyces sp. and demonstrated that the VapC toxin in this system can cross-activate TA operons in E. coli.
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Registered trials
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.