A MAMMALIAN HOMOLOG OF SEC61P AND SECYP IS ASSOCIATED WITH RIBOSOMES AND NASCENT POLYPEPTIDES DURING TRANSLOCATION
A MAMMALIAN HOMOLOG OF SEC61P AND SECYP IS ASSOCIATED WITH RIBOSOMES AND NASCENT POLYPEPTIDES DURING TRANSLOCATION
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DOI：
10.1016/0092-8674(92)90517-g
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发表时间：
1992-10-30
期刊：
影响因子：
64.5
通讯作者：
RAPOPORT, TA
中科院分区：
文献类型：
--
作者：
GORLICH, D;PREHN, S;RAPOPORT, TA
SEC61p是蛋白质跨酿酒酵母内质网膜转运所必需的。我们已经发现了一个哺乳动物同源物，它与酵母蛋白的序列同源性超过50%。此外，SEC61p的几个区域与细菌SecYp的相应区域有显著的相似性，表明蛋白质易位机制在进化上具有很强的保守性。哺乳动物的Sec61p和酵母蛋白一样，在新生多肽通过膜的过程中位于其附近。它与膜结合的核糖体紧密相关，这表明新生的链直接从核糖体进入蛋白质传导通道。这些结果将Sec61p定义为蛋白质转运器中普遍存在的关键组件。
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.