Endogenous ADP-ribosylation of elongation factor-2 by interleukin-1β

  title={Endogenous ADP-ribosylation of elongation factor-2 by interleukin-1β},
  author={Doris J{\"a}ger and Karl Werdan and Ursula Mueller-Werdan},
  journal={Molecular and Cellular Biochemistry},
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 (diphthamide715) within eEF-2, thus inactivating the enzyme… CONTINUE READING

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