ArticleProceedings of the National Academy of Sciences of the United States of America2013
Selectivity and self-assembly in the control of a bacterial toxin by an antitoxic noncoding RNA pseudoknot.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers, 1 of them a synthesis that pooled it.
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Who cites it
43 citing papers in PubMed, 1 synthesis or guideline pooled it, 74 citations in OpenAlex.
- A Systematic Overview of Type II and III Toxin-Antitoxin Systems with a Focus on Druggability.Toxins · 2018Pooled it
- Cryo-EM reveals the quaternary architecture of TenpIN type III toxin-antitoxin RNP complex common to pathogenic bacteria.PLoS pathogens · 2026Article
- Potential role of a CRISPR-Cas-activated toxin-antitoxin system in bacterial immunity.Nature communications · 2026Article
- The toxin-antitoxin complex Fic-1-AntF functions as a deAMPylase that regulates the activity of DNA gyrase.mLife · 2026Article
- Functional Coupling and Evolutionary Relationships Between Toxin-Antitoxin Systems and CRISPR-Cas Systems.Toxins · 2025Review
- Disassembly activates Retron-Septu for antiphage defense.Science (New York, N.Y.) · 2025Article
- Deciphering the RNA-based regulation mechanism of the phage-encoded AbiF system in Clostridioides difficile.PLoS genetics · 2025Article
- Bioinformatic exploration reveals features of tenpIN family of type III toxin-antitoxin systems in bacteria and viruses.Scientific reports · 2025Article
- Type II Toxin-Antitoxin Systems inInfection and drug resistance · 2025Review
- RNA-protein interaction prediction without high-throughput data: An overview and benchmark ofComputational and structural biotechnology journal · 2024Article
- Using nucleolytic toxins as restriction enzymes enables new RNA applications.Nucleic acids research · 2024Article
- Accurate prediction of RNA secondary structure including pseudoknots through solving minimum-cost flow with learned potentials.Communications biology · 2024Article
- Large-scale Purification of Type III Toxin-antitoxin Ribonucleoprotein Complex and its Components fromBio-protocol · 2023Article
- Toxin-antitoxin systems in bacterial pathogenesis.Heliyon · 2023Review
- Biology and evolution of bacterial toxin-antitoxin systems.Nature reviews. Microbiology · 2022Review
- Identification, functional characterization, assembly and structure of ToxIN type III toxin-antitoxin complex from E. coli.Nucleic acids research · 2022Article
- Shutoff of host transcription triggers a toxin-antitoxin system to cleave phage RNA and abort infection.Molecular cell · 2021Article
- The World of Stable Ribonucleoproteins and Its Mapping With Grad-Seq and Related Approaches.Frontiers in molecular biosciences · 2021Review
- Substrate specificity of bacterial endoribonuclease toxins.BMB reports · 2020Review
- A unified dinucleotide alphabet describing both RNA and DNA structures.Nucleic acids research · 2020Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Bacterial small RNAs perform numerous regulatory roles, including acting as antitoxic components in toxin-antitoxin systems. In type III toxin-antitoxin systems, small processed RNAs directly antagonize their toxin protein partners, and in the systems characterized the toxin and antitoxin components together form a trimeric assembly. In the present study, we sought to define how the RNA antitoxin, ToxI, inhibits its potentially lethal protein partner, ToxN. We show through cross-inhibition experiments with the ToxIN systems from Pectobacterium atrosepticum (ToxIN(Pa)) and Bacillus thuringiensis (ToxIN(Bt)) that ToxI RNAs are highly selective enzyme inhibitors. Both systems have an "addictive" plasmid maintenance phenotype. We demonstrate that ToxI(Pa) can inhibit ToxN(Pa) in vitro both in its processed form and as a repetitive precursor RNA, and this inhibition is linked to the self-assembly of the trimeric complex. Inhibition and self-assembly are both mediated entirely by the ToxI(Pa) RNA, with no requirement for cellular factors or exogenous energy. Finally, we explain the origins of ToxI antitoxin selectivity through our crystal structure of the ToxIN(Bt) complex. Our results show how a processed RNA pseudoknot can inhibit a deleterious protein with exquisite molecular specificity and how these self-contained and addictive RNA-protein pairs can confer different adaptive benefits in their bacterial hosts.
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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.