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Published online 23 August 2004. doi:10.1083/jcb.200405138
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 166, Number 5, 621-627
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 Two novel proteins in the mitochondrial outer membrane mediate ß-barrel protein assembly

Daigo Ishikawa1, Hayashi Yamamoto1, Yasushi Tamura1, Kaori Moritoh1, and Toshiya Endo1,2,3

1 Department of Chemistry, Graduate School of Science
2 Institute for Advanced Research, Japan Science and Technology Corporation, Nagoya University, Chikusa-ku, Nagoya 464-8602, Japan
3 Core Research for Evolutional Science and Technology, Japan Science and Technology Corporation, Nagoya University, Chikusa-ku, Nagoya 464-8602, Japan

Address correspondence to Toshiya Endo, Dept. of Chemistry, Graduate School of Science, Nagoya University, Chikusa-ku, Nagoya 464-8602, Japan. Tel.: 81-52-789-2490. Fax: 81-52-789-2947. email: endo{at}biochem.chem.nagoya-u.ac.jp


Abstract
Mitochondrial outer and inner membranes contain translocators that achieve protein translocation across and/or insertion into the membranes. Recent evidence has shown that mitochondrial ß-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, Tom13 and Tom38/Sam35, that mediate assembly of mitochondrial ß-barrel proteins, Tom40, and/or porin in the outer membrane. Depletion of Tom13 or Tom38/Sam35 affects assembly pathways of the ß-barrel proteins differently, suggesting that they mediate different steps of the complex assembly processes of ß-barrel proteins in the outer membrane.

Key Words: mitochondria; protein import; membrane protein assembly; yeast; translocator

Abbreviations used in this paper: AAC, ADP/ATP carrier; BN-PAGE, blue-native PAGE; PK, proteinase K; TIM, translocator of the mitochondrial inner membrane; TOM, translocator of the mitochondrial outer membrane.


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