Post-translational protein translocation into thylakoids by the Sec and ΔpH-dependent pathways

被引：90

作者：

Mori, H ^{[1
]}

Cline, K ^{[1
]}

机构：

[1] Univ Florida, Gainesville, FL 32611 USA

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH | 2001年 / 1541卷 / 1-2期

关键词：

Tat; twin arginine; folded protein transport; chloroplast; amphipathic helix; signal peptide;

D O I：

10.1016/S0167-4889(01)00150-1

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：

Two distinct protein translocation pathways that employ hydrophobic signal peptides function in the plant thylakoid membrane. These two systems are precursor specific and distinguished by their energy and component requirements. Recent studies have shown that one pathway is homologous to the bacterial general export system called Sec. The other one, called the Delta pH-dependent pathway, was originally considered to be unique to plant thylakoids. However, it is now known that homologous transport systems are widely present in prokaryotes and even present in archaea. Here we review these protein transport pathways and discuss their capabilities and mechanisms of operation. (C) 2001 Elsevier Science B.V. All rights reserved.

引用

页码：80 / 90

页数：11

共 87 条

[11] Potential receptor function of three homologous components, TatA, TatB and TatE, of the twin-arginine signal sequence-dependent metalloenzyme translocation pathway in Escherichia coli [J].