ArticleNucleic acids research2018
Escherichia coli ItaT is a type II toxin that inhibits translation by acetylating isoleucyl-tRNAIle.
Article in Nucleic acids research, 2018. 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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28 citing papers in PubMed, 42 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
- Disruption of sulfur transferase complex increases bacterial intramacrophage persistence.PLoS pathogens · 2025Article
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- Toxic small alarmone synthetase FaRel2 inhibits translation by pyrophosphorylating tRNAScience advances · 2024Article
- Nucleotidyltransferase toxin MenT extends aminoacyl acceptor ends of serine tRNAs to control Mycobacterium tuberculosis growth.Nature communications · 2024Article
- Toxic Small Alarmone Synthetase FaRel2 inhibits translation by pyrophosphorylating tRNAbioRxiv : the preprint server for biology · 2024Article
- MenT nucleotidyltransferase toxins extend tRNA acceptor stems and can be inhibited by asymmetrical antitoxin binding.Nature communications · 2023Article
- The DarT/DarG Toxin-Antitoxin ADP-Ribosylation System as a Novel Target for a Rational Design of Innovative Antimicrobial Strategies.Pathogens (Basel, Switzerland) · 2023Article
- The novel type II toxin-antitoxin PacTA modulates Pseudomonas aeruginosa iron homeostasis by obstructing the DNA-binding activity of Fur.Nucleic acids research · 2022Article
- Comparative Analysis of Diverse Acetyltransferase-Type Toxin-Antitoxin Loci in Klebsiella pneumoniae.Microbiology spectrum · 2022Article
- A tRNA-Acetylating Toxin and Detoxifying Enzyme in Mycobacterium tuberculosis.Microbiology spectrum · 2022Article
- GNAT toxins evolve toward narrow tRNA target specificities.Nucleic acids research · 2022Article
- Biology and evolution of bacterial toxin-antitoxin systems.Nature reviews. Microbiology · 2022Review
- Substrate recognition and cryo-EM structure of the ribosome-bound TAC toxin of Mycobacterium tuberculosis.Nature communications · 2022Article
- Auxiliary interfaces support the evolution of specific toxin-antitoxin pairing.Nature chemical biology · 2021Article
- AtaT Improves the Stability of Pore-Forming Protein EspB by Acetylating Lysine 206 to Enhance Strain Virulence.Frontiers in microbiology · 2021Article
- Bacterial type II toxin-antitoxin systems acting through post-translational modifications.Computational and structural biotechnology journal · 2021Review
- Substrate specificity of bacterial endoribonuclease toxins.BMB reports · 2020Review
- Modified base-binding EVE and DCD domains: striking diversity of genomic contexts in prokaryotes and predicted involvement in a variety of cellular processes.BMC biology · 2020Article
- Mechanism of aminoacyl-tRNA acetylation by an aminoacyl-tRNA acetyltransferase AtaT from enterohemorrhagic E. coli.Nature communications · 2020Article
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Authors and funding
14 authors at 6 institutions in 3 countries.
Funding
Abstract
Prokaryotic toxin-antitoxin (TA) modules are highly abundant and are involved in stress response and drug tolerance. The most common type II TA modules consist of two interacting proteins. The type II toxins are diverse enzymes targeting various essential intracellular targets. The antitoxin binds to cognate toxin and inhibits its function. Recently, TA modules whose toxins are GNAT-family acetyltransferases were described. For two such systems, the target of acetylation was shown to be aminoacyl-tRNA: the TacT toxin targets aminoacylated elongator tRNAs, while AtaT targets the amino acid moiety of initiating tRNAMet. We show that the itaRT gene pair from Escherichia coli encodes a TA module with acetyltransferase toxin ItaT that specifically and exclusively acetylates Ile-tRNAIle thereby blocking translation and inhibiting cell growth. ItaT forms a tight complex with the ItaR antitoxin, which represses the transcription of itaRT operon. A comprehensive bioinformatics survey of GNAT acetyltransferases reveals that enzymes encoded by validated or putative TA modules are common and form a distinct branch of the GNAT family tree. We speculate that further functional analysis of such TA modules will result in identification of enzymes capable of specifically targeting many, perhaps all, aminoacyl tRNAs.
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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.