ArticleNature structural & molecular biology2013
A bacterial toxin catalyzing tyrosine glycosylation of Rho and deamidation of Gq and Gi proteins.
Article in Nature structural & molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 67 citations in OpenAlex.
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- Tyrosine-modifying glycosylation by Yersinia effectors.The Journal of biological chemistry · 2024Article
- An Updated View on the Cellular Uptake and Mode-of-Action of Clostridioides difficile Toxins.Advances in experimental medicine and biology · 2024Article
- Glycosylating Effectors ofBiomolecules · 2022Review
- Posttranslational modification of the RHO of plants protein RACB by phosphorylation and cross-kingdom conserved ubiquitination.PloS one · 2022Article
- Detecting Glucose Fluctuations in theACS chemical biology · 2021Article
- Remodeling of host glycoproteins during bacterial infection.BMB reports · 2021Review
- Large Clostridial Toxins: Mechanisms and Roles in Disease.Microbiology and molecular biology reviews : MMBR · 2021Review
- Strategies towards Targeting Gαi/s Proteins: Scanning of Protein-Protein Interaction Sites To Overcome Inaccessibility.ChemMedChem · 2021Review
- Overcoming off-targets: assessing Western blot signals for Bcnt/Cfdp1, a tentative component of the chromatin remodeling complex.Bioscience reports · 2020Article
- Type III Secretion Effectors with Arginine N-Glycosyltransferase Activity.Microorganisms · 2020Review
- Inverse control of Rab proteins byScience advances · 2020Article
- TheThe Journal of biological chemistry · 2019Article
- A cysteine protease-like domain enhances the cytotoxic effects of theThe Journal of biological chemistry · 2019Article
- Synthesis of aryl-thioglycopeptides through chemoselective Pd-mediated conjugation.Chemical science · 2018Article
- The chaperonin TRiC/CCT is essential for the action of bacterial glycosylating protein toxins likeProceedings of the National Academy of Sciences of the United States of America · 2018Article
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Authors and funding
12 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Entomopathogenic Photorhabdus asymbiotica is an emerging pathogen in humans. Here, we identified a P. asymbiotica protein toxin (PaTox), which contains a glycosyltransferase and a deamidase domain. PaTox mono-O-glycosylates Y32 (or Y34) of eukaryotic Rho GTPases by using UDP-N-acetylglucosamine (UDP-GlcNAc). Tyrosine glycosylation inhibits Rho activation and prevents interaction with downstream effectors, resulting in actin disassembly, inhibition of phagocytosis and toxicity toward insects and mammalian cells. The crystal structure of the PaTox glycosyltransferase domain in complex with UDP-GlcNAc determined at 1.8-Å resolution represents a canonical GT-A fold and is the smallest glycosyltransferase toxin known. (1)H-NMR analysis identifies PaTox as a retaining glycosyltransferase. The glutamine-deamidase domain of PaTox blocks GTP hydrolysis of heterotrimeric Gαq/11 and Gαi proteins, thereby activating RhoA. Thus, PaTox hijacks host GTPase signaling in a bidirectional manner by deamidation-induced activation and glycosylation-induced inactivation of GTPases.
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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.