ArticleNucleic acids research2024
Toxin release by conditional remodelling of ParDE1 from Mycobacterium tuberculosis leads to gyrase inhibition.
Article in Nucleic acids research, 2024. 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.
- A haloarchaeal VapBC toxin-antitoxin system: regulatory mechanism and role in establishing population heterogeneity to facilitate survival of subpopulations under stress conditions.Applied and environmental microbiology · 2026Article
- Phosphorylation of PfiA modulates Pf4 phage production through PfiA/PfiT stoichiometric reconfiguration inScience advances · 2026Article
- Recent Characterization of Key Proteins to Combat Tuberculosis.Advances in experimental medicine and biology · 2026Review
- PglZ from Type I BREX phage defence systems is a metal-dependent nuclease that forms a sub-complex with BrxB.Nucleic acids research · 2025Article
- Broken beyond repair: TA system ParE toxins mediate effective gyrase inhibition without driving resistance.Journal of bacteriology · 2025Article
- Functional analysis of the type II toxin-antitoxin system ParDE in Streptococcus suis serotype 2.BMC veterinary research · 2025Article
- Conformational change as a mechanism for toxin activation in bacterial toxin-antitoxin systems.Journal of virology · 2024Review
- Inducible auto-phosphorylation regulates a widespread family of nucleotidyltransferase toxins.Nature communications · 2024Article
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Authors and funding
6 authors.
Funding
Abstract
Mycobacterium tuberculosis, the causative agent of tuberculosis, is a growing threat to global health, with recent efforts towards its eradication being reversed in the wake of the COVID-19 pandemic. Increasing resistance to gyrase-targeting second-line fluoroquinolone antibiotics indicates the necessity to develop both novel therapeutics and our understanding of M. tuberculosis growth during infection. ParDE toxin-antitoxin systems also target gyrase and are regulated in response to both host-associated and drug-induced stress during infection. Here, we present microbiological, biochemical, structural, and biophysical analyses exploring the ParDE1 and ParDE2 systems of M. tuberculosis H37Rv. The structures reveal conserved modes of toxin-antitoxin recognition, with complex-specific interactions. ParDE1 forms a novel heterohexameric ParDE complex, supported by antitoxin chains taking on two distinct folds. Curiously, ParDE1 exists in solution as a dynamic equilibrium between heterotetrameric and heterohexameric complexes. Conditional remodelling into higher order complexes can be thermally driven in vitro. Remodelling induces toxin release, tracked through concomitant inhibition and poisoning of gyrase activity. Our work aids our understanding of gyrase inhibition, allowing wider exploration of toxin-antitoxin systems as inspiration for potential therapeutic agents.
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