Cleavage of a tail-anchored protein by signal peptidase

被引：23

作者：

Nilsson, I

Johnson, AE

von Heijne, G ^{[2
]}

机构：

[1] Texas A&M Univ, Syst Hlth Sci Ctr, Dept Med Biochem & Genet, College Stn, TX 77843 USA

[2] Univ Stockholm, Dept Biochem & Biophys, SE-10691 Stockholm, Sweden

[3] Texas A&M Univ, Dept Biochem & Biophys, College Stn, TX 77843 USA

[4] Texas A&M Univ, Dept Chem, College Stn, TX 77843 USA

来源：

FEBS LETTERS | 2002年 / 516卷 / 1-3期

关键词：

membrane protein; signal peptide; signal peptidase; tail-anchor;

D O I：

10.1016/S0014-5793(02)02511-5

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：

Tail-anchored proteins are post-translationally targeted and inserted into the endoplasmic reticulum membrane. They do not use the co-translational sign at-recognition particle (SRP)-dependent pathway, but rather utilize an ill-defined, ATP-dependent mechanism. Here, we show that a tail-anchored protein can be cleaved by signal peptidase and that the sequence requirements for efficient cleavage seem to be the same as for cleavage of co-translationally targeted SRP-dependent proteins. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

引用

页码：106 / 108

页数：3

共 13 条

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Beilharz T, 2000, MOL BIOL CELL, V11, p207A

[2] Targeting of tail-anchored proteins to yeast mitochondria in vivo [J].