ArticleStructure (London, England : 1993)2014
CdiA from Enterobacter cloacae delivers a toxic ribosomal RNase into target bacteria.
Article in Structure (London, England : 1993), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
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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.
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Who cites it
60 citing papers in PubMed, 75 citations in OpenAlex.
- 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
- Molecular and structural basis of a subfamily of PrfH rescuing both the damaged and intact ribosomes stalled in translation.Science advances · 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
- Proteolytically activated antibacterial toxins inhibit the growth of diverse gram-positive bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Unveiling the multifaceted domain polymorphism of the Menshen antiphage system.Nucleic acids research · 2025Article
- Harnessing the human gut microbiota: an emerging frontier in combatting multidrug-resistant bacteria.Frontiers in immunology · 2025Review
- 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
- Antimicrobial Lasso Peptide Cloacaenodin Utilizes a Unique TonB-Dependent Transporter to Access Susceptible Bacteria.ACS chemical biology · 2024Article
- Paradoxical Activation of a Type VI Secretion System Phospholipase Effector by Its Cognate Immunity Protein.Journal of bacteriology · 2023Article
- Structural basis for the toxic activity of MafB2 from maf genomic island 2 (MGI-2) in N. meningitidis B16B6.Scientific reports · 2023Article
- Intercepting biological messages: Antibacterial molecules targeting nucleic acids during interbacterial conflicts.Genetics and molecular biology · 2023Article
- Ribonuclease T2 represents a distinct circularly permutated version of the BECR RNases.Protein science : a publication of the Protein Society · 2023Article
- Proteolytic processing induces a conformational switch required for antibacterial toxin delivery.Nature communications · 2022Article
- Sequential rescue and repair of stalled and damaged ribosome by bacterial PrfH and RtcB.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Functional and Structural Diversity of Bacterial Contact-Dependent Growth Inhibition Effectors.Frontiers in molecular biosciences · 2022Review
- Cryptic Genes for Interbacterial Antagonism DistinguishFrontiers in cellular and infection microbiology · 2022Article
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7 authors at 2 institutions in 1 country.
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Abstract
Contact-dependent growth inhibition (CDI) is one mechanism of inter-bacterial competition. CDI(+) cells export large CdiA effector proteins, which carry a variety of C-terminal toxin domains (CdiA-CT). CdiA-CT toxins are specifically neutralized by cognate CdiI immunity proteins to protect toxin-producing cells from autoinhibition. Here, we use structure determination to elucidate the activity of a CDI toxin from Enterobacter cloacae (ECL). The structure of CdiA-CT(ECL) resembles the C-terminal nuclease domain of colicin E3, which cleaves 16S ribosomal RNA to disrupt protein synthesis. In accord with this structural homology, we show that CdiA-CT(ECL) uses the same nuclease activity to inhibit bacterial growth. Surprisingly, although colicin E3 and CdiA(ECL) carry equivalent toxin domains, the corresponding immunity proteins are unrelated in sequence, structure, and toxin-binding site. Together, these findings reveal unexpected diversity among 16S rRNases and suggest that these nucleases are robust and versatile payloads for a variety of toxin-delivery platforms.
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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.