Jank, Thomas and Bogdanovic, Xenia and Wirth, Christophe and Haaf, Erik and Spoerner, Michael and Boehmer, Kira E. and Steinemann, Marcus and Orth, Joachim H. C. and Kalbitzer, Hans Robert and Warscheid, Bettina and Hunte, Carola and Aktories, Klaus (2013) A bacterial toxin catalyzing tyrosine glycosylation of Rho and deamidation of G(q) and G(i) proteins. NATURE STRUCTURAL & MOLECULAR BIOLOGY, 20 (11). pp. 1273-1280. ISSN 1545-9993, 1545-9985
Full text not available from this repository. (Request a copy)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-angstrom resolution represents a canonical GT-A fold and is the smallest glycosyltransferase toxin known. H-1-NMR analysis identifies PaTox as a retaining glycosyltransferase. The glutamine-deamidase domain of PaTox blocks GTP hydrolysis of heterotrimeric G alpha(q/11) and G alpha(i) proteins, thereby activating RhoA. Thus, PaTox hijacks host GTPase signaling in a bidirectional manner by deamidation-induced activation and glycosylation-induced inactivation of GTPases.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | PHOTORHABDUS-LUMINESCENS; HA-RAS; ACTIVATION; SALMONELLA; DOMAIN; HOST; GLUCOSYLATION; CONSEQUENCES; ASYMBIOTICA; REFINEMENT; |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 25 Mar 2020 10:40 |
| Last Modified: | 25 Mar 2020 10:40 |
| URI: | https://pred.uni-regensburg.de/id/eprint/15751 |
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