Frolova L, Le Goff X, Rasmussen H H, Cheperegin S, Drugeon G, Kress M, Arman I, Haenni A L, Celis J E, Philippe M
Department of Molecular Biology, University of Aarhus, Denmark.
Nature. 1994 Dec 15;372(6507):701-3. doi: 10.1038/372701a0.
The termination of protein synthesis in ribosomes is governed by termination (stop) codons in messenger RNAs and by polypeptide chain release factors (RFs). Although the primary structure of prokaryotic RFs and yeast mitochrondrial RF is established, that of the only known eukaryotic RF (eRF) remains obscure. Here we report the assignment of a family of tightly related proteins (designated eRF1) from lower and higher eukaryotes which are structurally and functionally similar to rabbit eRF. Two of these proteins, one from human and the other from Xenopus laevis, have been expressed in yeast and Escherichia coli, respectively, purified and shown to be active in the in vitro RF assay. The other protein of this family, sup45 (sup1) of Saccharomyces cerevisiae, is involved in omnipotent suppression during translation. The amino-acid sequence of the eRF1 family is highly conserved. We conclude that the eRF1 proteins are directly implicated in the termination of translation in eukaryotes.
核糖体中蛋白质合成的终止由信使核糖核酸中的终止（密码子）密码子以及多肽链释放因子（RFs）控制。尽管原核生物RFs和酵母线粒体RF的一级结构已确定，但唯一已知的真核生物RF（eRF）的一级结构仍不清楚。在此，我们报告了来自低等和高等真核生物的一族紧密相关的蛋白质（命名为eRF1），它们在结构和功能上与兔eRF相似。其中两种蛋白质，一种来自人类，另一种来自非洲爪蟾，已分别在酵母和大肠杆菌中表达、纯化，并在体外RF测定中显示具有活性。该家族的另一种蛋白质，酿酒酵母的sup45（sup1），参与翻译过程中的全能抑制。eRF1家族的氨基酸序列高度保守。我们得出结论，eRF1蛋白直接参与真核生物翻译的终止。
