Journal
MOLECULAR AND CELLULAR BIOCHEMISTRY
Volume 348, Issue 1-2, Pages 125-128Publisher
SPRINGER
DOI: 10.1007/s11010-010-0646-8
Keywords
Elongation factor-2; Interleukin-1 beta; ADP-ribosylation; Cytokines; Protein synthesis
Categories
Funding
- Deutsche Forschungsgemeinschaft
- Bundesministerium fur Bildung und Forschung
Ask authors/readers for more resources
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-1 beta (IL-1 beta). Thereby, systemic inflammatory processes may link to protein synthesis regulation.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available