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First published online July 10, 2003
doi: 10.1242/10.1242/jcs.00667


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Journal of Cell Science 116, 3259-3267 (2003)
doi: 10.1242/jcs.00667


Commentary

Functional cooperation and separation of translocators in protein import into mitochondria, the double-membrane bounded organelles

Toshiya Endo1,2,*, Hayashi Yamamoto1 and Masatoshi Esaki1

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

* Author for correspondence (e-mail: endo{at}biochem.chem.nagoya-u.ac.jp)

Nearly all mitochondrial proteins are synthesized in the cytosol and subsequently imported into mitochondria with the aid of translocators: the TOM complex in the outer membrane, and the TIM23 and TIM22 complexes in the inner membrane. The TOM complex and the TIM complexes cooperate to achieve efficient transport of proteins to the matrix or into the inner membrane and several components, including Tom22, Tim23, Tim50 and small Tim proteins, mediate functional coupling of the two translocator systems. The TOM complex can be disconnected from the TIM systems and their energy sources (ATP and {Delta}{Psi}), however, using alternative mechanisms to achieve vectorial protein translocation across the outer membrane

Key words: Mitochondria, Protein import, Translocator, TOM, TIM




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