Newly synthesized mitochondrial proteins are imported into mitochondria with the aid of protein translocator complexes in the outer and inner mitochondrial membranes. We report the identification of yeast Tam41, a new member of mitochondrial protein translocator systems. Tam41 is a peripheral inner mitochondrial membrane protein facing the matrix. Disruption of the TAM41 gene led to temperature-sensitive growth of yeast cells and resulted in defects in protein import via the TIM23 translocator complex at elevated temperature both in vivo and in vitro. Although Tam41 is not a constituent of the TIM23 complex, depletion of Tam41 led to a decreased molecular size of the TIM23 complex and partial aggregation of Pam18 and -16. Import of Pam16 into mitochondria without Tam41 was retarded, and the imported Pam16 formed aggregates in vitro. These results suggest that Tam41 facilitates mitochondrial protein import by maintaining the functional integrity of the TIM23 protein translocator complex from the matrix side of the inner membrane.
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28 August 2006
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August 28 2006
Identification of Tam41 maintaining integrity of the TIM23 protein translocator complex in mitochondria
Yasushi Tamura,
Yasushi Tamura
1Department of Chemistry, Graduate School of Science
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Yoshihiro Harada,
Yoshihiro Harada
1Department of Chemistry, Graduate School of Science
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Koji Yamano,
Koji Yamano
1Department of Chemistry, Graduate School of Science
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Kazuaki Watanabe,
Kazuaki Watanabe
1Department of Chemistry, Graduate School of Science
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Daigo Ishikawa,
Daigo Ishikawa
1Department of Chemistry, Graduate School of Science
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Chié Ohshima,
Chié Ohshima
1Department of Chemistry, Graduate School of Science
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Shuh-ichi Nishikawa,
Shuh-ichi Nishikawa
1Department of Chemistry, Graduate School of Science
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Hayashi Yamamoto,
Hayashi Yamamoto
1Department of Chemistry, Graduate School of Science
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Toshiya Endo
Toshiya Endo
1Department of Chemistry, Graduate School of Science
2Institute for Advanced Research,
3Core Research for Evolutional Science and Technology, Japan Science and Technology Corporation, Nagoya University, Chikusa-ku, Nagoya 464-8602, Japan
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Yasushi Tamura
1Department of Chemistry, Graduate School of Science
Yoshihiro Harada
1Department of Chemistry, Graduate School of Science
Koji Yamano
1Department of Chemistry, Graduate School of Science
Kazuaki Watanabe
1Department of Chemistry, Graduate School of Science
Daigo Ishikawa
1Department of Chemistry, Graduate School of Science
Chié Ohshima
1Department of Chemistry, Graduate School of Science
Shuh-ichi Nishikawa
1Department of Chemistry, Graduate School of Science
Hayashi Yamamoto
1Department of Chemistry, Graduate School of Science
Toshiya Endo
1Department of Chemistry, Graduate School of Science
2Institute for Advanced Research,
3Core Research for Evolutional Science and Technology, Japan Science and Technology Corporation, Nagoya University, Chikusa-ku, Nagoya 464-8602, Japan
Correspondence to Toshiya Endo: [email protected]
Y. Tamura and Y. Harada contributed equally to this paper.
Abbreviations used in this paper: BN-PAGE, blue-native PAGE; DHFR, dihydrofolate reductase; IMS, intermembrane space; MMC, mitochondrial Hsp70–associated motor and chaperone; PK, proteinase K; WT, wild-type.
Received:
March 17 2006
Accepted:
July 27 2006
Online ISSN: 1540-8140
Print ISSN: 0021-9525
The Rockefeller University Press
2006
J Cell Biol (2006) 174 (5): 631–637.
Article history
Received:
March 17 2006
Accepted:
July 27 2006
Citation
Yasushi Tamura, Yoshihiro Harada, Koji Yamano, Kazuaki Watanabe, Daigo Ishikawa, Chié Ohshima, Shuh-ichi Nishikawa, Hayashi Yamamoto, Toshiya Endo; Identification of Tam41 maintaining integrity of the TIM23 protein translocator complex in mitochondria . J Cell Biol 28 August 2006; 174 (5): 631–637. doi: https://doi.org/10.1083/jcb.200603087
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