Signal peptidase and oligosaccharyltransferase interact in a sequential and dependent manner within the endoplasmic reticulum

被引：39

作者：

Chen, XM ^{[1
]}

VanValkenburgh, C ^{[1
]}

Liang, HB ^{[1
]}

Fang, H ^{[1
]}

Green, N ^{[1
]}

机构：

[1] Vanderbilt Univ, Sch Med, Dept Microbiol & Immunol, Nashville, TN 37232 USA

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2001年 / 276卷 / 04期

关键词：

D O I：

10.1074/jbc.M007723200

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：

We demonstrate that the signal peptides of prepro-alpha -factor and preinvertase must be cleaved before Asn-X-Ser/Thr acceptor tripeptides located near the signal peptides of these precursors can be efficiently glycosylated within the endoplasmic reticulum of the yeast Saccharomyces cerevisiae. The data support a model whereby the interaction of a signal peptide with the membrane prevents an acceptor tripeptide juxtaposed to the signal peptide from accessing the oligosaccharyltransferase active site until the signal peptide is cleaved.

引用

页码：2411 / 2416

页数：6

共 21 条

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