ArticleNucleic acids research2017
Structure of a novel antibacterial toxin that exploits elongation factor Tu to cleave specific transfer RNAs.
Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 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
26 citing papers in PubMed, 32 citations in OpenAlex.
- Pathogenic Bordetella Bacteria Exploit Axonemal Microtubules to Penetrate the Ciliary Barrier.Cytoskeleton (Hoboken, N.J.) · 2026Article
- Elongation Factor Tu Acts as a Chaperone to Activate an Antibacterial RNase Toxin.Molecular microbiology · 2026Article
- The yxiD gene from Bacillus subtilis 6633 encodes a polymorphic toxin with tRNase activity and is neutralized by the cognate immunity protein YxxD.Nucleic acids research · 2025Article
- Mechanism of activation of contact-dependent growth inhibition tRNase toxin by the amino acid biogenesis factor CysK in the bacterial competition system.Nucleic acids research · 2025Article
- Thioredoxin 1 moonlights as a chaperone for an interbacterial ADP-ribosyltransferase toxin.Nature communications · 2024Article
- Systematic discovery of antibacterial and antifungal bacterial toxins.Nature microbiology · 2024Article
- Contact-dependent growth inhibition (CDI) systems deploy a large family of polymorphic ionophoric toxins for inter-bacterial competition.PLoS genetics · 2024Article
- Metabolic Labeling: Snapshot of the Effect of Toxins on the Key Cellular Processes.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Paradoxical Activation of a Type VI Secretion System Phospholipase Effector by Its Cognate Immunity Protein.Journal of bacteriology · 2023Article
- Recent insights into the structure and function of coronavirus ribonucleases.FEBS open bio · 2022Review
- Proteolytic processing induces a conformational switch required for antibacterial toxin delivery.Nature communications · 2022Article
- Mechanistic insights into tRNA cleavage by a contact-dependent growth inhibitor protein and translation factors.Nucleic acids research · 2022Article
- Functional and Structural Diversity of Bacterial Contact-Dependent Growth Inhibition Effectors.Frontiers in molecular biosciences · 2022Review
- Genomic discovery and structural dissection of a novel type of polymorphic toxin system in gram-positive bacteria.Computational and structural biotechnology journal · 2022Article
- Article
- Article
- tRNA 3' shortening by LCCR4 as a response to stress in Trypanosoma brucei.Nucleic acids research · 2021Article
- Contact-Dependent Growth Inhibition in Bacteria: Do Not Get Too Close!International journal of molecular sciences · 2020Review
- Polymorphic Toxins and Their Immunity Proteins: Diversity, Evolution, and Mechanisms of Delivery.Annual review of microbiology · 2020Review
- Role of Recipient Susceptibility Factors During Contact-Dependent Interbacterial Competition.Frontiers in microbiology · 2020Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
11 authors at 3 institutions in 1 country.
Funding
Abstract
Contact-dependent growth inhibition (CDI) is a mechanism of inter-cellular competition in which Gram-negative bacteria exchange polymorphic toxins using type V secretion systems. Here, we present structures of the CDI toxin from Escherichia coli NC101 in ternary complex with its cognate immunity protein and elongation factor Tu (EF-Tu). The toxin binds exclusively to domain 2 of EF-Tu, partially overlapping the site that interacts with the 3'-end of aminoacyl-tRNA (aa-tRNA). The toxin exerts a unique ribonuclease activity that cleaves the single-stranded 3'-end from tRNAs that contain guanine discriminator nucleotides. EF-Tu is required to support this tRNase activity in vitro, suggesting the toxin specifically cleaves substrate in the context of GTP·EF-Tu·aa-tRNA complexes. However, superimposition of the toxin domain onto previously solved GTP·EF-Tu·aa-tRNA structures reveals potential steric clashes with both aa-tRNA and the switch I region of EF-Tu. Further, the toxin induces conformational changes in EF-Tu, displacing a β-hairpin loop that forms a critical salt-bridge contact with the 3'-terminal adenylate of aa-tRNA. Together, these observations suggest that the toxin remodels GTP·EF-Tu·aa-tRNA complexes to free the 3'-end of aa-tRNA for entry into the nuclease active site.
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.