Sorting and assembly of mitochondrial outer membrane proteins

被引:50
作者
Becker, Thomas [1 ]
Voegtle, F. Nora. [1 ]
Stojanovski, Diana [1 ]
Meisinger, Chris [1 ]
机构
[1] Univ Freiburg, Inst Biochem & Mol Biol, Zentrum Biochem & Mol Zellforsch, D-79104 Freiburg, Germany
来源
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS | 2008年 / 1777卷 / 7-8期
关键词
protein import; assembly; SAM; TOM; morphology;
D O I
10.1016/j.bbabio.2008.03.017
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
In the last years the picture of protein import into the mitochondria has become much more complicated in terms of new components and new sorting pathways. These novel findings have also changed views concerning the biogenesis pathway of mitochondrial outer membrane proteins. In addition to proteins anchored with transmembrane alpha-helices, the endosymbiotic origin of the mitochondria has resulted in the presence of transmembrane beta-barrels in this compartment. The sorting and assembly pathway of outer membrane Proteins involves three machineries: the translocase of the outer membrane (TOM complex) the sorting and assembly machinery (SAM complex) and the MDM complex (mitochondrial distribution and morphology). Here we review recent developments on the biogenesis pathways of outer membrane proteins with a focus on Tom proteins, the most intensively studied class of these precursor proteins. (C) 2008 Elsevier B.V. All rights reserved.
引用
收藏
页码:557 / 563
页数:7
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