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

Daigo Ishikawa, Hayashi Yamamoto, Yasushi Tamura, Kaori Moritoh, Toshiya Endo

Department of Chemistry, Graduate School of Science, Nagoya University, Chikusa-ku, Nagoya 464-8602, Japan.

The Journal of cell biology 2004 Aug 30

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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, Tom13 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.

Citation

Daigo Ishikawa, Hayashi Yamamoto, Yasushi Tamura, Kaori Moritoh, Toshiya Endo. Two novel proteins in the mitochondrial outer membrane mediate beta-barrel protein assembly. The Journal of cell biology. 2004 Aug 30;166(5):621-7