期刊
MOLECULAR AND CELLULAR BIOCHEMISTRY
卷 348, 期 1-2, 页码 125-128出版社
SPRINGER
DOI: 10.1007/s11010-010-0646-8
关键词
Elongation factor-2; Interleukin-1 beta; ADP-ribosylation; Cytokines; Protein synthesis
类别
资金
- Deutsche Forschungsgemeinschaft
- Bundesministerium fur Bildung und Forschung
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.
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