Structural insight into the mitochondrial protein import system

被引:113
作者
Endo, Toshiya [1 ]
Yamano, Koji [1 ]
Kawano, Shin [1 ]
机构
[1] Nagoya Univ, Dept Chem, Grad Sch Sci, Chikusa Ku, Nagoya, Aichi 4648602, Japan
来源
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES | 2011年 / 1808卷 / 03期
关键词
Protein import; Mitochondria; Translocator; Receptor; X-ray structure; NMR structure; TIM23 PREPROTEIN TRANSLOCASE; INTERMEMBRANE SPACE PROTEINS; DEPENDENT SULFHYDRYL OXIDASE; DISULFIDE RELAY SYSTEM; C-TERMINAL DOMAIN; OUTER-MEMBRANE; INNER MEMBRANE; CRYSTAL-STRUCTURE; YEAST MITOCHONDRIA; PRESEQUENCE TRANSLOCASE;
D O I
10.1016/j.bbamem.2010.07.018
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
Mitochondrial functions rely on precise and efficient transport of 1000-1500 different mitochondrial proteins from the cytosol to appropriate mitochondria! subcompartments. Those mitochondrial protein transport processes are mediated by the dedicated mitochondrial protein import system comprised of translocators in the outer and inner mitochondrial membranes and soluble factors in the cytosol, intermembrane space, and matrix. In the last decade, high-resolution structures of many of the components of the mitochondrial protein import machineries have become available, which has significantly advanced our understanding of the molecular mechanisms of mitochondrial protein transport. Here we review the currently available high-resolution structures of the components of the mitochondrial protein import machineries that afford structural and mechanistic insight into how the mitochondrial import system works. This article is part of a Special Issue entitled Protein translocation across or insertion into membranes. (C) 2010 Elsevier B.V. All rights reserved.
引用
收藏
页码:955 / 970
页数:16
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