A MAMMALIAN HOMOLOG OF SEC61P AND SECYP IS ASSOCIATED WITH RIBOSOMES AND NASCENT POLYPEPTIDES DURING TRANSLOCATION

被引：386

作者：

GORLICH, D ^{[1
]}

PREHN, S ^{[1
]}

HARTMANN, E ^{[1
]}

KALIES, KU ^{[1
]}

RAPOPORT, TA ^{[1
]}

机构：

[1] HUMBOLDT UNIV,INST BIOCHEM,O-1040 BERLIN,GERMANY

来源：

CELL | 1992年 / 71卷 / 03期

关键词：

D O I：

10.1016/0092-8674(92)90517-G

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：489 / 503

页数：15

共 56 条

[1] RIBOSOME-MEMBRANE INTERACTION - NONDESTRUCTIVE DISASSEMBLY OF RAT-LIVER ROUGH MICROSOMES INTO RIBOSOMAL AND MEMBRANOUS COMPONENTS [J].