Characterization of the enzymatic activity of Clostridium perfringens TpeL
| Autor: | Jean Claude Rousselle, Serge Pauillac, Jacques D'allayer, Pascal Lenormand, Philippe Bouvet, Michel R. Popoff |
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| Přispěvatelé: | Bactéries anaérobies et Toxines, Institut Pasteur [Paris], Protéomique (Plate-Forme), This was supported by Institut Pasteur funding, Institut Pasteur [Paris] (IP) |
| Jazyk: | angličtina |
| Rok vydání: | 2013 |
| Předmět: |
Clostridium perfringens
[ SDV.TOX ] Life Sciences [q-bio]/Toxicology MESH: rac GTP-Binding Proteins Toxicology medicine.disease_cause Substrate Specificity Rho-GTPases Tandem Mass Spectrometry TpeL Chromatography High Pressure Liquid chemistry.chemical_classification MESH: Clostridium perfringens 0303 health sciences Uridine Diphosphate N-Acetylglucosamine MESH : Substrate Specificity rac GTP-Binding Proteins Biochemistry [SDV.TOX]Life Sciences [q-bio]/Toxicology MESH : Tandem Mass Spectrometry MESH: ras Proteins Gene isoform MESH : Clostridium perfringens Bacterial Toxins Biology 03 medical and health sciences MESH : Chromatography High Pressure Liquid MESH : Uridine Diphosphate N-Acetylglucosamine Rho MESH: Uridine Diphosphate N-Acetylglucosamine medicine MESH: Chromatography High Pressure Liquid GTPase 030304 developmental biology 030306 microbiology Toxin Rho GTPases MESH: Tandem Mass Spectrometry MESH : rac GTP-Binding Proteins Molecular biology In vitro Rac carbohydrates (lipids) Enzyme Rac glucosylation chemistry MESH: Bacterial Toxins MESH : Bacterial Toxins ras Proteins MESH: Substrate Specificity MESH : ras Proteins Ras |
| Zdroj: | Toxicon Toxicon, Elsevier, 2013, 75, pp.136-143. 〈10.1016/j.toxicon.2013.07.003〉 Toxicon, Elsevier, 2013, 75, pp.136-143. ⟨10.1016/j.toxicon.2013.07.003⟩ Toxicon, 2013, 75, pp.136-143. ⟨10.1016/j.toxicon.2013.07.003⟩ |
| ISSN: | 0041-0101 |
| Popis: | International audience; TpeL is a toxin produced by Clostridium perfringens which belongs to the large clostridial glucosylating toxin family. It was shown that TpeL modifies Ras using UDP-glucose or UDP-N-acetylglucosamine as cosubstrates (Guttenberg et al., 2012; Nagahama et al., 2011). We confirmed that TpeL preferentially glucosaminates the three isoforms of Ras (cH-Ras, N-Ras, and K-Ras) from UDP-N-acetylglucosamine and to a lower extent Rap1a and R-Ras3, and very weakly Rac1. In contrast to previous report, we observed that Ral was not a substrate of TpeL. In addition, we confirmed by in vitro glucosylation and mass spectrometry that TpeL modifies cH-Ras at Thr35. |
| Databáze: | OpenAIRE |
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