A mammalian homolog of SEC61p and SECYp is associated with ribosomes and nascent polypeptides during translocation

Dirk Görlich*, Siegfried Prehn, Enno Hartmann, Kai Uwe Kalies, Tom A. Rapoport

*Corresponding author for this work
317 Citations (Scopus)

Abstract

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.

Original languageEnglish
JournalCell
Volume71
Issue number3
Pages (from-to)489-503
Number of pages15
ISSN0092-8674
DOIs
Publication statusPublished - 30.10.1992

Fingerprint

Dive into the research topics of 'A mammalian homolog of SEC61p and SECYp is associated with ribosomes and nascent polypeptides during translocation'. Together they form a unique fingerprint.

Cite this