ArticleNucleic acids research2017
The CDI toxin of Yersinia kristensenii is a novel bacterial member of the RNase A superfamily.
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 24 papers.
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Who cites it
24 citing papers in PubMed, 30 citations in OpenAlex.
- Article
- The Pseudomonas aeruginosa ribonuclease Ribocin cleaves eukaryotic ribosomes at helix 69 to inhibit host translation.PLoS biology · 2026Article
- Elongation Factor Tu Acts as a Chaperone to Activate an Antibacterial RNase Toxin.Molecular microbiology · 2026Article
- Bacteria deliver a microtubule-binding protein into mammalian cells to promote colonization.Science (New York, N.Y.) · 2026Article
- The dominant lineage of an emerging pathogen harbours contact-dependent inhibition systems.Microbial genomics · 2025Article
- Contact-dependent growth inhibition (CDI) systems deploy a large family of polymorphic ionophoric toxins for inter-bacterial competition.PLoS genetics · 2024Article
- Structural basis for the toxic activity of MafB2 from maf genomic island 2 (MGI-2) in N. meningitidis B16B6.Scientific reports · 2023Article
- Ribonuclease T2 represents a distinct circularly permutated version of the BECR RNases.Protein science : a publication of the Protein Society · 2023Article
- 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
- Polymorphic Toxins and Their Immunity Proteins: Diversity, Evolution, and Mechanisms of Delivery.Annual review of microbiology · 2020Review
- An ancient evolutionary connection between Ribonuclease A and EndoU families.RNA (New York, N.Y.) · 2020Article
- Molecular and Biochemical Characterization of YeeF/YezG, a Polymorphic Toxin-Immunity Protein Pair FromFrontiers in microbiology · 2020Article
- Target highlights in CASP13: Experimental target structures through the eyes of their authors.Proteins · 2019Article
- Convergent Evolution of the Barnase/EndoU/Colicin/RelE (BECR) Fold in Antibacterial tRNase Toxins.Structure (London, England : 1993) · 2019Article
- The Cytoplasm-Entry Domain of Antibacterial CdiA Is a Dynamic α-Helical Bundle with Disulfide-Dependent Structural Features.Journal of molecular biology · 2019Article
- Article
- Testing a Human Antimicrobial RNase Chimera Against Bacterial Resistance.Frontiers in microbiology · 2019Article
- Conservation of Dynamics Associated with Biological Function in an Enzyme Superfamily.Structure (London, England : 1993) · 2018Article
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Authors and funding
10 authors at 4 institutions in 1 country.
Funding
Abstract
Contact-dependent growth inhibition (CDI) is an important mechanism of inter-bacterial competition found in many Gram-negative pathogens. CDI+ cells express cell-surface CdiA proteins that bind neighboring bacteria and deliver C-terminal toxin domains (CdiA-CT) to inhibit target-cell growth. CDI+ bacteria also produce CdiI immunity proteins, which specifically neutralize cognate CdiA-CT toxins to prevent self-inhibition. Here, we present the crystal structure of the CdiA-CT/CdiIYkris complex from Yersinia kristensenii ATCC 33638. CdiA-CTYkris adopts the same fold as angiogenin and other RNase A paralogs, but the toxin does not share sequence similarity with these nucleases and lacks the characteristic disulfide bonds of the superfamily. Consistent with the structural homology, CdiA-CTYkris has potent RNase activity in vitro and in vivo. Structure-guided mutagenesis reveals that His175, Arg186, Thr276 and Tyr278 contribute to CdiA-CTYkris activity, suggesting that these residues participate in substrate binding and/or catalysis. CdiIYkris binds directly over the putative active site and likely neutralizes toxicity by blocking access to RNA substrates. Significantly, CdiA-CTYkris is the first non-vertebrate protein found to possess the RNase A superfamily fold, and homologs of this toxin are associated with secretion systems in many Gram-negative and Gram-positive bacteria. These observations suggest that RNase A-like toxins are commonly deployed in inter-bacterial competition.
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