The Twin-Arginine Protein Franslocation Pathway

被引：118

作者：

Berks, Ben C. ^{[1
]}

机构：

[1] Univ Oxford, Dept Biochem, Oxford OX1 3QU, England

来源：

ANNUAL REVIEW OF BIOCHEMISTRY, VOL 84 | 2015年 / 84卷

基金：

英国生物技术与生命科学研究理事会; 英国医学研究理事会;

关键词：

protein transport; twin-arginine; membrane protein; signal peptide; bacterial protein export; thylakoid import; SIGNAL PEPTIDE BINDING; CYSTEINE-SCANNING MUTAGENESIS; TRANSLOCASE TATC COMPONENT; FOLDING QUALITY-CONTROL; ESCHERICHIA-COLI TATA; TRANSPORT-SYSTEM; BACILLUS-SUBTILIS; EXPORT PATHWAY; THYLAKOID MEMBRANE; PRECURSOR-BINDING;

D O I：

10.1146/annurev-biochem-060614-034251

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

070307 [化学生物学]; 071010 [生物化学与分子生物学];

摘要：

The twin-arginine translocation (Tat) system, found in prokaryotes, chloroplasts, and sonic mitochondria, allows folded proteins to be moved across membranes. How this transport is achieved without significant ion leakage is an intriguing mechanistic question. Tat transport is mediated by complexes formed from small integral membrane proteins from just two protein families. Atomic-resolution structures have recently been determined for representatives of both these protein families, providing the first molecular-level glimpse of the Tat machinery. I review our current understanding of the mechanism of Tat transport in light of these new structural data.

引用

收藏

页码：843 / 864

页数：22

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