ArticleCommunications biology2020
Characterization of a toxin-antitoxin system in Mycobacterium tuberculosis suggests neutralization by phosphorylation as the antitoxicity mechanism.
Article in Communications biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 56 citations in OpenAlex.
- The toxin-antitoxin complex Fic-1-AntF functions as a deAMPylase that regulates the activity of DNA gyrase.mLife · 2026Article
- Recent Characterization of Key Proteins to Combat Tuberculosis.Advances in experimental medicine and biology · 2026Review
- The Prevalence and Diversity of Marine Toxin-Antitoxin Systems.Marine drugs · 2025Article
- Heterologous expression of the M. abscessus CBASS system confers phage TM4 resistance in M. smegmatis.BMC microbiology · 2025Article
- Bacterial programmed cell death and toxin-antitoxin system in bacteria.Archives of microbiology · 2025Review
- Ser/Thr phosphorylation ofmBio · 2025Article
- Investigation of potential relationship betweenmazEF3, relJK, and vapBC3 genes and antimicrobial resistance inMycobacterium bovis.BMC infectious diseases · 2025Article
- Type II Toxin-Antitoxin Systems inInfection and drug resistance · 2025Review
- Type I toxin-antitoxin systems in bacteria: from regulation to biological functions.EcoSal Plus · 2024Review
- Structural and Evolutionary Analysis of Proteins Endowed with a Nucleotidyltransferase, or Non-canonical Palm, Catalytic Domain.Journal of molecular evolution · 2024Article
- Nucleotidyltransferase toxin MenT extends aminoacyl acceptor ends of serine tRNAs to control Mycobacterium tuberculosis growth.Nature communications · 2024Article
- CRISPR Screening and Comparative LC-MS Analysis Identify Genes Mediating Efficacy of Delamanid and Pretomanid against Mycobacterium tuberculosis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Long Dynamic β1-β2 Loops inInternational journal of molecular sciences · 2024Article
- Inducible auto-phosphorylation regulates a widespread family of nucleotidyltransferase toxins.Nature communications · 2024Article
- The Toxin of VapBC-1 Toxin-Antitoxin Module fromMicroorganisms · 2024Article
- Mycobacterium tuberculosis strain with deletions in menT3 and menT4 is attenuated and confers protection in mice and guinea pigs.Nature communications · 2024Article
- Substrate specificity of Mycobacterium tuberculosis tRNA terminal nucleotidyltransferase toxin MenT3.Nucleic acids research · 2024Article
- PCR Development for Analysis of Some Type II Toxin-Antitoxin Systems, relJK, mazEF3, and vapBC3 Genes, in Mycobacterium tuberculosis and Mycobacterium bovis.Current microbiology · 2024Article
- Distribution of lineages and type II toxin-antitoxin systems among rifampin-resistant Mycobacterium Tuberculosis Isolates.PloS one · 2024Article
- Identification of Genes Encoded Toxin-Antitoxin System inInfectious disorders drug targets · 2024Article
Corrections and comments
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Authors and funding
11 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mycobacterium tuberculosis (Mtb) encodes an exceptionally large number of toxin-antitoxin (TA) systems, supporting the hypothesis that TA systems are involved in pathogenesis. We characterized the putative Mtb Rv1044-Rv1045 TA locus structurally and functionally, demonstrating that it constitutes a bona fide TA system but adopts a previously unobserved antitoxicity mechanism involving phosphorylation of the toxin. While Rv1045 encodes the guanylyltransferase TglT functioning as a toxin, Rv1044 encodes the novel atypical serine protein kinase TakA, which specifically phosphorylates the cognate toxin at residue S78, thereby neutralizing its toxicity. In contrast to previous predictions, we found that Rv1044-Rv1045 does not belong to the type IV TA family because TglT and TakA interact with each other as substrate and kinase, suggesting an unusual type of TA system. Protein homology analysis suggests that other COG5340-DUF1814 protein pairs, two highly associated but uncharacterized protein families widespread in prokaryotes, might share this unusual antitoxicity mechanism.
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