ArticleThe Journal of biological chemistry2010
Noncognate Mycobacterium tuberculosis toxin-antitoxins can physically and functionally interact.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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Who cites it
52 citing papers in PubMed, 78 citations in OpenAlex.
- Structural and functional characterization of VapBC52 toxin-antitoxin system from Mycobacterium tuberculosis.Nucleic acids research · 2026Article
- VapC36-mediated intrinsic stress adaption is required for copper tolerance and pathogenesis ofScience advances · 2026Article
- Protein-Protein Interactions as Promising Molecular Targets for Novel Antimicrobials Aimed at Gram-Negative Bacteria.International journal of molecular sciences · 2025Review
- Understanding the physiological role and cross-interaction network of VapBC35 toxin-antitoxin system from Mycobacterium tuberculosis.Communications biology · 2025Article
- Phosphorylation of VapB antitoxins affects intermolecular interactions to regulate VapC toxin activity inJournal of bacteriology · 2024Article
- Type II and IV toxin-antitoxin systems coordinately stabilize the integrative and conjugative element of the ICESa2603 family conferring multiple drug resistance in Streptococcus suis.PLoS pathogens · 2024Article
- MazEF Homologs inToxins · 2024Article
- The Benefits of Toxicity:Microorganisms · 2023Article
- Factorization and pseudofactorization of weighted graphs.Discrete applied mathematics (Amsterdam, Netherlands : 1988) · 2023Article
- The structural basis of hyperpromiscuity in a core combinatorial network of type II toxin-antitoxin and related phage defense systems.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Bacterial Toxin-Antitoxin Systems' Cross-Interactions-Implications for Practical Use in Medicine and Biotechnology.Toxins · 2023Review
- Bacterial toxin-antitoxin systems: Novel insights on toxin activation across populations and experimental shortcomings.Current research in microbial sciences · 2023Review
- tRNAAntimicrobial agents and chemotherapy · 2022Article
- Identification and characterization of VapBC toxin-antitoxin system inRNA (New York, N.Y.) · 2021Article
- Rapid Identification of Secondary Structure and Binding Site Residues in an Intrinsically Disordered Protein Segment.Frontiers in genetics · 2021Article
- Review
- Article
- Review
- VapC21 Toxin Contributes to Drug-Tolerance and Interacts With Non-cognate VapB32 Antitoxin inFrontiers in microbiology · 2020Article
- Bioinformatic and mutational studies of related toxin-antitoxin pairs inThe Journal of biological chemistry · 2019Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The Mycobacterium tuberculosis genome harbors a striking number (>40) of toxin-antitoxin systems. Among them are at least seven MazF orthologs, designated MazF-mt1 through MazF-mt7, four of which have been demonstrated to function as mRNA interferases that selectively target mRNA for cleavage at distinct consensus sequences. As is characteristic of all toxin-antitoxin systems, each of the mazF-mt toxin genes is organized in an operon downstream of putative antitoxin genes. However, only one of the seven putative upstream antitoxins (designated MazE-mt1 through MazE-mt7) has significant sequence similarity to Escherichia coli MazE, the cognate antitoxin for E. coli MazF. Interestingly, the M. tuberculosis genome contains two independent operons encoding E. coli MazE orthologs, but they are not paired with mazF-mt-like genes. Instead, the genes encoding these two MazE orthologs are each paired with proteins containing a PIN domain, indicating that they may be members of the very large VapBC toxin-antitoxin family. We tested a spectrum of pair-wise combinations of cognate and noncognate Mtb toxin-antitoxins using in vivo toxicity and rescue experiments along with in vitro interaction experiments. Surprisingly, we uncovered several examples of noncognate toxin-antitoxin association, even among different families (e.g. MazF toxins and VapB antitoxins). These results challenge the "one toxin for one antitoxin" dogma and suggest that M. tuberculosis may enlist a sophisticated toxin-antitoxin network to alter its physiology in response to environmental cues.
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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.