ArticleNature communications2022
Mechanism of threonine ADP-ribosylation of F-actin by a Tc toxin.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 22 citations in OpenAlex.
- Discovery of a fungal Tc toxin complex and functional mycoserpin through a novel two-by-two comparative genomics approach.Frontiers in cellular and infection microbiology · 2026Article
- Structure of the F-tractin-F-actin complex.The Journal of cell biology · 2025Article
- Multistate kinetics of the syringe-like injection mechanism of Tc toxins.Science advances · 2025Article
- Antagonistic Effects of Actin-Specific Toxins onBiomolecules · 2024Article
- Review
- Antagonistic effects of actin-specific toxins onbioRxiv : the preprint server for biology · 2024Article
- A deep learning method to predict bacterial ADP-ribosyltransferase toxins.Bioinformatics (Oxford, England) · 2024Article
- Article
- Molecular basis of threonine ADP-ribosylation of ubiquitin by bacterial ARTs.Nature chemical biology · 2024Article
- Yersinia entomophaga Tc toxin is released by T10SS-dependent lysis of specialized cell subpopulations.Nature microbiology · 2024Article
- Crystal structure of bacterial ubiquitin ADP-ribosyltransferase CteC reveals a substrate-recruiting insertion.The Journal of biological chemistry · 2024Article
- Stepwise assembly and release of Tc toxins from Yersinia entomophaga.Nature microbiology · 2024Article
- Structure and activation mechanism of the Makes caterpillars floppy 1 toxin.Nature communications · 2023Article
- Structures of the Insecticidal Toxin Complex Subunit XptA2 Highlight Roles for Flexible Domains.International journal of molecular sciences · 2023Article
- Recent insights into mechanisms of cellular toxicity and cell recognition associated with the ABC family of pore-forming toxins.Biochemical Society transactions · 2023Article
- The DarT/DarG Toxin-Antitoxin ADP-Ribosylation System as a Novel Target for a Rational Design of Innovative Antimicrobial Strategies.Pathogens (Basel, Switzerland) · 2023Article
- Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tc toxins deliver toxic enzymes into host cells by a unique injection mechanism. One of these enzymes is the actin ADP-ribosyltransferase TccC3, whose activity leads to the clustering of the cellular cytoskeleton and ultimately cell death. Here, we show in atomic detail how TccC3 modifies actin. We find that the ADP-ribosyltransferase does not bind to G-actin but interacts with two consecutive actin subunits of F-actin. The binding of TccC3 to F-actin occurs via an induced-fit mechanism that facilitates access of NAD
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