ArticleNucleic acids research2015
Molecular basis of ribosome recognition and mRNA hydrolysis by the E. coli YafQ toxin.
Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- The HigB-like SehA toxin promotes non-replicating Salmonella inside macrophages by inhibiting ribonuclease III-dependent rRNA maturation.Nucleic acids research · 2026Article
- An RNA modification prevents extended codon-anticodon interactions from facilitating +1 frameshifting.Nature communications · 2025Article
- Article
- Type II Toxin-Antitoxin Systems inInfection and drug resistance · 2025Review
- Strategies to Investigate Membrane Damage, Nucleoid Condensation, and RNase Activity of Bacterial Toxin-Antitoxin Systems.Methods and protocols · 2021Article
- Genome Sequencing of fiveMicroorganisms · 2021Article
- A YoeB toxin cleaves both RNA and DNA.Scientific reports · 2021Article
- Substrate specificity of bacterial endoribonuclease toxins.BMB reports · 2020Review
- Rapid growth inhibitory activity of a YafQ-family endonuclease toxin of the Helicobacter pylori tfs4 integrative and conjugative element.Scientific reports · 2020Article
- Distinct oligomeric structures of the YoeB-YefM complex provide insights into the conditional cooperativity of type II toxin-antitoxin system.Nucleic acids research · 2020Article
- Role of Toxin-Antitoxin-Regulated Persister Population and Indole in Bacterial Heat Tolerance.Applied and environmental microbiology · 2020Article
- The Positively Charged Active Site of the Bacterial Toxin RelE Causes a Large Shift in the General Base pBiochemistry · 2020Article
- The Variety in the Common Theme of Translation Inhibition by Type II Toxin-Antitoxin Systems.Frontiers in genetics · 2020Review
- Identifying a Molecular Mechanism That Imparts Species-Specific Toxicity to YoeB Toxins.Frontiers in microbiology · 2020Article
- Monomeric YoeB toxin retains RNase activity but adopts an obligate dimeric form for thermal stability.Nucleic acids research · 2019Article
- Expression of DinJ-YafQ System ofMicroorganisms · 2019Article
- Toxin-antitoxin operon kacAT of Klebsiella pneumoniae is regulated by conditional cooperativity via a W-shaped KacA-KacT complex.Nucleic acids research · 2019Article
- Identification and first characterization of DinJ-YafQ toxin-antitoxin systems in Lactobacillus species of biotechnological interest.Scientific reports · 2019Article
- The toxin from a ParDE toxin-antitoxin system found in Pseudomonas aeruginosa offers protection to cells challenged with anti-gyrase antibiotics.Molecular microbiology · 2019Article
- Genotoxic, Metabolic, and Oxidative Stresses Regulate the RNA Repair Operon of Salmonella enterica Serovar Typhimurium.Journal of bacteriology · 2018Article
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4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial type II toxin-antitoxin modules are protein-protein complexes whose functions are finely tuned by rapidly changing environmental conditions. E. coli toxin YafQ is suppressed under steady state growth conditions by virtue of its interaction with its cognate antitoxin, DinJ. During stress, DinJ is proteolytically degraded and free YafQ halts translation by degrading ribosome-bound mRNA to slow growth until the stress has passed. Although structures of the ribosome with toxins RelE and YoeB have been solved, it is unclear what residues among ribosome-dependent toxins are essential for mediating both recognition of the ribosome and the mRNA substrate given their low sequence identities. Here we show that YafQ coordinates binding to the 70S ribosome via three surface-exposed patches of basic residues that we propose directly interact with 16S rRNA. We demonstrate that YafQ residues H50, H63, D67 and H87 participate in acid-base catalysis during mRNA hydrolysis and further show that H50 and H63 functionally complement as general bases to initiate the phosphodiester cleavage reaction. Moreover YafQ residue F91 likely plays an important role in mRNA positioning. In summary, our findings demonstrate the plasticity of ribosome-dependent toxin active site residues and further our understanding of which toxin residues are important for function.
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