Kisselev L L, Buckingham R H
Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, 32 Vavilova, 117984, Moscow, Russia.
Trends Biochem Sci. 2000 Nov;25(11):561-6. doi: 10.1016/s0968-0004(00)01669-8.
Translational termination has been a largely ignored aspect of protein synthesis for many years. However, the recent identification of new release-factor genes, the mapping of release-factor functional sites and in vitro reconstitution experiments have provided a deeper understanding of the termination mechanism. In addition, protein-protein interactions among release factors and with other proteins have been revealed. The three-dimensional structures of a prokaryotic ribosome recycling factor and eukaryotic release factor 1 (eRF1) mimic the shape of transfer RNA, indicating that they bind to the same ribosomal site. Post-termination events in bacteria have been clarified, linking termination, ribosomal recycling and translation initiation.
多年来，翻译终止一直是蛋白质合成中一个很大程度上被忽视的方面。然而，最近新释放因子基因的鉴定、释放因子功能位点的定位以及体外重组实验，让人们对终止机制有了更深入的理解。此外，还揭示了释放因子之间以及与其他蛋白质之间的蛋白质-蛋白质相互作用。原核核糖体循环因子和真核释放因子1（eRF1）的三维结构模仿了转运RNA的形状，这表明它们与核糖体的同一位点结合。细菌中的终止后事件已经得到阐明，将终止、核糖体循环和翻译起始联系了起来。
