ArticleThe Journal of biological chemistry2016
Functional Diversity of Cytotoxic tRNase/Immunity Protein Complexes from Burkholderia pseudomallei.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 31 citations in OpenAlex.
- 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
- 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
- Proteolytic processing induces a conformational switch required for antibacterial toxin delivery.Nature communications · 2022Article
- Cryptic Genes for Interbacterial Antagonism DistinguishFrontiers in cellular and infection microbiology · 2022Article
- Functional and Structural Diversity of Bacterial Contact-Dependent Growth Inhibition Effectors.Frontiers in molecular biosciences · 2022Review
- Conservation of binding properties in protein models.Computational and structural biotechnology journal · 2021Article
- Polymorphic Toxins and Their Immunity Proteins: Diversity, Evolution, and Mechanisms of Delivery.Annual review of microbiology · 2020Review
- Molecular and Biochemical Characterization of YeeF/YezG, a Polymorphic Toxin-Immunity Protein Pair FromFrontiers in microbiology · 2020Article
- Convergent Evolution of the Barnase/EndoU/Colicin/RelE (BECR) Fold in Antibacterial tRNase Toxins.Structure (London, England : 1993) · 2019Article
- Combination of SAXS and Protein Painting Discloses the Three-Dimensional Organization of the Bacterial Cysteine Synthase Complex, a Potential Target for Enhancers of Antibiotic Action.International journal of molecular sciences · 2019Article
- The Cytoplasm-Entry Domain of Antibacterial CdiA Is a Dynamic α-Helical Bundle with Disulfide-Dependent Structural Features.Journal of molecular biology · 2019Article
- Burkholderia cepacia Complex Contact-Dependent Growth Inhibition Systems Mediate Interbacterial Competition.Journal of bacteriology · 2019Article
- CDI/CDS system-encoding genes of Burkholderia thailandensis are located in a mobile genetic element that defines a new class of transposon.PLoS genetics · 2019Article
- Contact-dependent interbacterial toxins deliver a message.Current opinion in microbiology · 2018Review
- Template-based quaternary structure prediction of proteins using enhanced profile-profile alignments.Proteins · 2018Article
- Evaluation of the template-based modeling in CASP12.Proteins · 2018Article
- Introducing the new bacterial branch of the RNase A superfamily.RNA biology · 2018Article
- Structure of a novel antibacterial toxin that exploits elongation factor Tu to cleave specific transfer RNAs.Nucleic acids research · 2017Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Contact-dependent growth inhibition (CDI) is a widespread mechanism of inter-bacterial competition. CDI(+) bacteria deploy large CdiA effector proteins, which carry variable C-terminal toxin domains (CdiA-CT). CDI(+) cells also produce CdiI immunity proteins that specifically neutralize cognate CdiA-CT toxins to prevent auto-inhibition. Here, we present the crystal structure of the CdiA-CT/CdiI(E479) toxin/immunity protein complex from Burkholderia pseudomallei isolate E479. The CdiA-CT(E479) tRNase domain contains a core α/β-fold that is characteristic of PD(D/E)XK superfamily nucleases. Unexpectedly, the closest structural homolog of CdiA-CT(E479) is another CDI toxin domain from B. pseudomallei 1026b. Although unrelated in sequence, the two B. pseudomallei nuclease domains share similar folds and active-site architectures. By contrast, the CdiI(E479) and CdiI(1026b) immunity proteins share no significant sequence or structural homology. CdiA-CT(E479) and CdiA-CT(1026b) are both tRNases; however, each nuclease cleaves tRNA at a distinct position. We used a molecular docking approach to model each toxin bound to tRNA substrate. The resulting models fit into electron density envelopes generated by small-angle x-ray scattering analysis of catalytically inactive toxin domains bound stably to tRNA. CdiA-CT(E479) is the third CDI toxin found to have structural homology to the PD(D/E)XK superfamily. We propose that CDI systems exploit the inherent sequence variability and active-site plasticity of PD(D/E)XK nucleases to generate toxin diversity. These findings raise the possibility that many other uncharacterized CDI toxins may belong to the PD(D/E)XK superfamily.
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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.