ArticleCell stress & chaperones2013
TAC from Mycobacterium tuberculosis: a paradigm for stress-responsive toxin-antitoxin systems controlled by SecB-like chaperones.
Article in Cell stress & chaperones, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 44 citations in OpenAlex.
- Proteomic insights into a M. tuberculosis clinical isolate with an increased propensity to form viable but non-replicating subpopulations during acid stress.Scientific reports · 2026Article
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- Bacterial toxin-antitoxin systems: Novel insights on toxin activation across populations and experimental shortcomings.Current research in microbial sciences · 2023Review
- Substrate recognition and cryo-EM structure of the ribosome-bound TAC toxin of Mycobacterium tuberculosis.Nature communications · 2022Article
- Coexpressing the Signal Peptide of Vip3A and the Trigger Factor ofFrontiers in microbiology · 2022Article
- The DisorderedMicroorganisms · 2021Article
- HigB1 Toxin inFrontiers in microbiology · 2021Article
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- Genomic and Proteomic Characterization of the Extended-Spectrum β-Lactamase (ESBL)-ProducingMicroorganisms · 2020Article
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- Novel Sequence Feature of SecA Translocase Protein Unique to the Thermophilic Bacteria: Bioinformatics Analyses to Investigate Their Potential Roles.Microorganisms · 2019Article
- TASmania: A bacterial Toxin-Antitoxin Systems database.PLoS computational biology · 2019Article
- Structural insights into chaperone addiction of toxin-antitoxin systems.Nature communications · 2019Article
- Directed evolution of SecB chaperones toward toxin-antitoxin systems.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Bottleneck in secretion of α-amylase in Bacillus subtilis.Microbial cell factories · 2017Review
- Physical and Functional Interplay between MazFApplied and environmental microbiology · 2017Article
- Chaperones in maturation of molybdoenzymes: Why specific is better than general?Bioengineered · 2017Article
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- Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial type II toxin-antitoxins (TAs) are two-component systems that modulate growth in response to specific stress conditions, thus promoting adaptation and persistence. The major human pathogen Mycobacterium tuberculosis potentially encodes 75 TAs and it has been proposed that persistence induced by active toxins might be relevant for its pathogenesis. In this work, we focus on the newly discovered toxin-antitoxin-chaperone (TAC) system of M. tuberculosis, an atypical stress-responsive TA system tightly controlled by a molecular chaperone that shows similarity to the canonical SecB chaperone involved in Sec-dependent protein export in Gram-negative bacteria. We performed a large-scale genome screening to reconstruct the evolutionary history of TAC systems and found that TAC is not restricted to mycobacteria and seems to have disseminated in diverse taxonomic groups by horizontal gene transfer. Our results suggest that TAC chaperones are evolutionary related to the solitary chaperone SecB and have diverged to become specialized toward their cognate antitoxins.
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