Two novel proteins in the mitochondrial outer membrane mediate β-barrel protein assembly

被引：128

作者：

Ishikawa, D

Yamamoto, H

Tamura, Y

Moritoh, K

Endo, T ^{[1
]}

机构：

[1] Nagoya Univ, Grad Sch Sci, Dept Chem, Chikusa Ku, Nagoya, Aichi 4648602, Japan

[2] Nagoya Univ, Inst Adv Res, Chikusa Ku, Nagoya, Aichi 4648602, Japan

[3] Nagoya Univ, Core Res Evolut Sci & Technol, Japan Sci & Technol Corp, Chikusa Ku, Nagoya, Aichi 4648602, Japan

来源：

JOURNAL OF CELL BIOLOGY | 2004年 / 166卷 / 05期

关键词：

mitochondria; protein import; membrane protein assembly; yeast; translocator;

D O I：

10.1083/jcb.200405138

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Mitochondrial outer and inner membranes contain translocators that achieve protein translocation across and/or insertion into the membranes. Recent evidence has shown that mitochondrial beta-barrel protein assembly in the outer membrane requires specific translocator proteins in addition to the components of the general translocator complex in the outer membrane, the TOM40 complex. Here we report two novel mitochondrial outer membrane proteins in yeast, Tom-beta and Tom38/Sam35, that mediate assembly of mitochondrial beta-barrel proteins, Tom40, and/or porin in the outer membrane. Depletion of Tom13 or Tom38/Sam35 affects assembly pathways of the beta-barrel proteins differently, suggesting that they mediate different steps of the complex assembly processes of beta-barrel proteins in the outer membrane.

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收藏

页码：621 / 627

页数：7

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