ReviewWiley interdisciplinary reviews. RNA2019
Toxins targeting transfer RNAs: Translation inhibition by bacterial toxin-antitoxin systems.
Review in Wiley interdisciplinary reviews. RNA, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
20 citing papers in PubMed, 22 citations in OpenAlex.
- A type VI secretion ADP-ribosyltransferase Rhs toxin selectively modifies charged tRNAThr(GGU) anticodon loops to block ACC codon decoding.Nucleic acids research · 2026Article
- BaCas12a3 represents a new subtype of type V CRISPR effector with collateral activity toward tRNA.Nucleic acids research · 2026Article
- Bacterial Persister Cells as Evolutionary Catalysts of Antibiotic Resistance: Mechanisms, Clinical Implications, and Therapeutic Strategies.Antibiotics (Basel, Switzerland) · 2026Review
- The selfish ribosome.PLoS biology · 2026Article
- The selfish ribosome.ArXiv · 2026Article
- Functional Coupling and Evolutionary Relationships Between Toxin-Antitoxin Systems and CRISPR-Cas Systems.Toxins · 2025Review
- Interpreting ribosome dynamics during mRNA translation.The Journal of biological chemistry · 2025Review
- Toxic small alarmone synthetase FaRel2 inhibits translation by pyrophosphorylating tRNAScience advances · 2024Article
- Deciphering the role of VapBC13 and VapBC26 toxin antitoxin systems in the pathophysiology of Mycobacterium tuberculosis.Communications biology · 2024Article
- Toxic Small Alarmone Synthetase FaRel2 inhibits translation by pyrophosphorylating tRNAbioRxiv : the preprint server for biology · 2024Article
- Characterization ofMicroorganisms · 2023Article
- The life and times of a tRNA.RNA (New York, N.Y.) · 2023Review
- Membrane lipid and expression responses ofFrontiers in microbiology · 2023Article
- Genomic Characterization ofFrontiers in microbiology · 2022Article
- Identification and characterization of VapBC toxin-antitoxin system inRNA (New York, N.Y.) · 2021Article
- Profiling the Virulence and Antibiotic Resistance Genes ofFrontiers in microbiology · 2021Article
- AtaT Improves the Stability of Pore-Forming Protein EspB by Acetylating Lysine 206 to Enhance Strain Virulence.Frontiers in microbiology · 2021Article
- Functional genomics reveals the toxin-antitoxin repertoire and AbiE activity inMicrobial genomics · 2020Article
- Recent Advances in Surface Nanoengineering for Biofilm Prevention and Control. Part I: Molecular Basis of Biofilm Recalcitrance. Passive Anti-Biofouling Nanocoatings.Nanomaterials (Basel, Switzerland) · 2020Review
- Toxin-mediated ribosome stalling reprograms the Mycobacterium tuberculosis proteome.Nature communications · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Prokaryotic toxin-antitoxin (TA) systems are composed of a protein toxin and its cognate antitoxin. These systems are abundant in bacteria and archaea and play an important role in growth regulation. During favorable growth conditions, the antitoxin neutralizes the toxin's activity. However, during conditions of stress or starvation, the antitoxin is inactivated, freeing the toxin to inhibit growth and resulting in dormancy. One mechanism of growth inhibition used by several TA systems results from targeting transfer RNAs (tRNAs), either through preventing aminoacylation, acetylating the primary amino group, or endonucleolytic cleavage. All of these mechanisms inhibit translation and result in growth arrest. Many of these toxins only act on a specific tRNA or a specific subset of tRNAs; however, more work is necessary to understand the specificity determinants of these toxins. For the toxins whose specificity has been characterized, both sequence and structural components of the tRNA appear important for recognition by the toxin. Questions also remain regarding the mechanisms used by dormant bacteria to resume growth after toxin induction. Rescue of stalled ribosomes by transfer-messenger RNAs, removal of acetylated amino groups from tRNAs, or ligation of cleaved RNA fragments have all been implicated as mechanisms for reversing toxin-induced dormancy. However, the mechanisms of resuming growth after induction of the majority of tRNA targeting toxins are not yet understood. This article is categorized under: Translation > Translation Regulation RNA in Disease and Development > RNA in Disease RNA Interactions with Proteins and Other Molecules > Protein-RNA Recognition.
Indexed as
Identifiers
What OpenQuestion holds
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.