THE 68-KDA PROTEIN OF SIGNAL RECOGNITION PARTICLE CONTAINS A GLYCINE-RICH REGION ALSO FOUND IN CERTAIN RNA-BINDING PROTEINS

被引：24

作者：

HERZ, J ^{[1
]}

FLINT, N ^{[1
]}

STANLEY, K ^{[1
]}

FRANK, R ^{[1
]}

DOBBERSTEIN, B ^{[1
]}

机构：

[1] EUROPEAN MOLEC BIOL LAB,POSTFACH 102209,W-6900 HEIDELBERG,GERMANY

来源：

FEBS LETTERS | 1990年 / 276卷 / 1-2期

关键词：

SIGNAL RECOGNITION PARTICLE; TRANSLOCATION; RIBONUCLEOPROTEIN PARTICLE; GLYCINE-RICH;

D O I：

10.1016/0014-5793(90)80518-N

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：

Signal recognition particle (SRP) interacts with the signal sequence in nascent secretory and membrane proteins and directs them to the membrane of the endoplasmic reticulum. Membrane targeting is mediated by the 68 and the 72 kDa proteins of SRP. We have cloned and sequenced cDNA encoding the 68 kDa protein of canine signal recognition particle (SRP68). SRP68 is a basic protein comprised of 622 amino acid residues. Close to the amino terminus there is a glycine-rich region which SRP68 has in common with some RNA-binding proteins. SRP68 shares no detectable similarity to any of the proteins in data libraries.

引用

页码：103 / 107

页数：5

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