Endogenous ADP-ribosylation of elongation factor-2 by interleukin-1β
| Autor: | Karl Werdan, Doris Jäger, Ursula Müller-Werdan |
|---|---|
| Rok vydání: | 2010 |
| Předmět: |
Virulence Factors
Bacterial Toxins Interleukin-1beta Clinical Biochemistry Exotoxins Endogeny Biology Ribosome Peptide Elongation Factor 2 Protein biosynthesis Animals Humans Transferase Histidine Myocytes Cardiac Molecular Biology Cells Cultured ADP Ribose Transferases Diphtheria toxin Activator (genetics) Cell Biology General Medicine Recombinant Proteins Rats Elongation factor Animals Newborn Biochemistry Protein Biosynthesis ADP-ribosylation Protein Processing Post-Translational |
| Zdroj: | Molecular and Cellular Biochemistry. 348:125-128 |
| ISSN: | 1573-4919 0300-8177 |
| DOI: | 10.1007/s11010-010-0646-8 |
| Popis: | Eukaryotic elongation factor-2 (eEF-2) catalyses the motion of the growing peptide chain relative to the mRNA at the ribosomes during protein synthesis. This highly conserved G-protein is the specific target of two lethal bacterial toxins, Pseudomonas aeruginosa exotoxin A and diphtheria toxin. These toxins exert their detrimental action by ADP-ribosylating a biologically unique posttranslationally modified histidine residue (diphthamide(715)) within eEF-2, thus inactivating the enzyme. Diphthamide(715) is also the target of endogenous (mono) ADP-ribosyl transferase activity. In this article, we report the first known activator of endogenous ADP-ribosylation of eEF-2, interleukin-1β (IL-1β). Thereby, systemic inflammatory processes may link to protein synthesis regulation. |
| Databáze: | OpenAIRE |
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