Department of Medicine III, University Halle-Wittenberg, Halle, Germany.
Mol Cell Biochem. 2011 Feb;348(1-2):125-8. doi: 10.1007/s11010-010-0646-8. Epub 2010 Nov 19.
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.
真核延伸因子-2（eEF-2）在蛋白质合成过程中催化核糖体上生长肽链相对于 mRNA 的运动。这种高度保守的 G 蛋白是两种致命细菌毒素——铜绿假单胞菌外毒素 A 和白喉毒素的特定靶标。这些毒素通过 ADP-ribosylating 修饰 eEF-2 内的一个生物独特的翻译后修饰组氨酸残基（二氢噻吩酰胺（715））发挥其有害作用，从而使酶失活。二氢噻吩酰胺（715）也是内源性（单）ADP-ribosyl 转移酶活性的靶标。在本文中，我们报道了第一个已知的 eEF-2 内源性 ADP-ribosylation 的激活剂，白细胞介素-1β（IL-1β）。由此，全身炎症过程可能与蛋白质合成调节有关。
