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Published 28 August 2006. doi:10.1083/jcb.200603087
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 174, Number 5, 631-637
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Identification of Tam41 maintaining integrity of the TIM23 protein translocator complex in mitochondria



Yasushi Tamura1, Yoshihiro Harada1, Koji Yamano1, Kazuaki Watanabe1, Daigo Ishikawa1, Chié Ohshima1, Shuh-ichi Nishikawa1, Hayashi Yamamoto1, and Toshiya Endo1,2,3

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

Correspondence to Toshiya Endo: endo{at}biochem.chem.nagoya-u.ac.jp

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.

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.


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