Görlich D, Prehn S, Hartmann E, Kalies K U, Rapoport T A
Max Delbrück Center for Molecular Medicine, Berlin-Buch, Germany.
Cell. 1992 Oct 30;71(3):489-503. doi: 10.1016/0092-8674(92)90517-g.
SEC61p is essential for protein translocation across the endoplasmic reticulum membrane of S. cerevisiae. We have found a mammalian homolog that shows more than 50% sequence identity with the yeast protein. Moreover, several regions of SEC61p have significant similarities with corresponding ones of SecYp of bacteria, indicating a strong evolutionary conservation of the mechanism of protein translocation. Mammalian Sec61p, like the yeast protein, is located in the immediate vicinity of nascent polypeptides during their membrane passage. It is tightly associated with membrane-bound ribosomes, suggesting that the nascent chain passes directly from the ribosome into a protein-conducting channel. These results define Sec61p as a ubiquitous key component of the protein translocation apparatus.
SEC61p对于蛋白质跨酿酒酵母内质网膜的转运至关重要。我们发现了一种哺乳动物同源物，它与酵母蛋白具有超过50%的序列同一性。此外，SEC61p的几个区域与细菌SecYp的相应区域有显著相似性，这表明蛋白质转运机制具有很强的进化保守性。与酵母蛋白一样，哺乳动物Sec61p在新生多肽通过膜的过程中位于其紧邻区域。它与膜结合核糖体紧密相连，这表明新生链直接从核糖体进入蛋白质传导通道。这些结果将Sec61p定义为蛋白质转运装置中普遍存在的关键组分。
