Hershey J W
Department of Biological Chemistry, School of Medicine, University of California, Davis.
Enzyme. 1990;44(1-4):17-27. doi: 10.1159/000468744.
Protein synthesis is controlled by the phosphorylation of proteins comprising the translational apparatus. At least 12 initiation factor polypeptides, 3 elongation factors and a ribosomal protein are implicated. Stimulation of translation correlates with enhanced phosphorylation of eIF-4F, eIF-4B, eIF-2B, eIF-3 and ribosomal protein S6, whereas inhibition correlates with phosphorylation of eEF-2 and the alpha-subunit of eIF-2. Strong evidence for regulatory roles exists for eIF-2, eIF-4F and eEF-2, whereas changes in other factor activities due to phosphorylation remain to be demonstrated. Regulation of the specific activity of the translational apparatus by phosphorylation appears to be a general mechanism for the control of rates of global protein synthesis, and may also play a role in modulating the translation of specific mRNAs.
蛋白质合成受组成翻译装置的蛋白质磷酸化作用的控制。至少涉及12种起始因子多肽、3种延伸因子和一种核糖体蛋白。翻译的刺激与eIF-4F、eIF-4B、eIF-2B、eIF-3和核糖体蛋白S6的磷酸化增强相关,而抑制则与eEF-2和eIF-2的α亚基的磷酸化相关。有强有力的证据表明eIF-2、eIF-4F和eEF-2具有调节作用,而其他因子活性因磷酸化而发生的变化仍有待证实。通过磷酸化对翻译装置的比活性进行调节似乎是控制整体蛋白质合成速率的一种普遍机制,并且可能在调节特定mRNA的翻译中也发挥作用。