STRUCTURE AND BIOSYNTHESIS OF THE SIGNAL-SEQUENCE RECEPTOR

被引：52

作者：

PREHN, S

HERZ, J

HARTMANN, E

KURZCHALIA, TV

FRANK, R

ROEMISCH, K

DOBBERSTEIN, B

RAPOPORT, TA

机构：

[1] EUROPEAN MOLEC BIOL LAB,W-6900 HEIDELBERG,GERMANY

[2] ACAD SCI GDR,ZENT INST MOLEK BIOL,O-1086 BERLIN,GERMANY

来源：

EUROPEAN JOURNAL OF BIOCHEMISTRY | 1990年 / 188卷 / 02期

关键词：

D O I：

10.1111/j.1432-1033.1990.tb15421.x

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：

The signal‐sequence receptor (SSR) has previously been shown to be a component of the environment which nascent polypeptides meet on passage through the endoplasmic reticulum (ER) membrane. We report here on the primary structure of the SSR as deduced from cDNA clones and from direct protein sequencing. The glycoprotein is synthesized with a cleavable amino‐terminal signal sequence and contains only one classical membrane‐spanning segment. Its insertion into the ER membrane during biosynthesis depends on the function of the signal‐recognition particle. SSR shows a remarkable charge distribution with the amino terminus being highly negatively charged, and the cytoplasmic carboxyl terminus positively charged. The SSR can be phosphorylated in its cytoplasmic tail both in intact cells and in a cell‐free system, suggesting a regulation of its function. The localization of the protein in the ER membrane was confirmed by immunofluorescence microscopy. Copyright © 1990, Wiley Blackwell. All rights reserved

引用

页码：439 / 445

页数：7

共 41 条

[1] INTERNAL AMINO-ACID SEQUENCE-ANALYSIS OF PROTEINS SEPARATED BY ONE-DIMENSIONAL OR TWO-DIMENSIONAL GEL-ELECTROPHORESIS AFTER INSITU PROTEASE DIGESTION ON NITROCELLULOSE [J].