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J. Biochem, 1998, Vol. 123, No. 6 1010-1016
© 1998 Japanese Biochemical Society


review-article

Mitochondria-Targeting Sequence, a Multi-Role Sorting Sequence Recognized at All Steps of Protein Import into Mitochondria

Tsuneo Omura1

Department of Molecular Biology, Graduate School of Medical Science, Kyushu University Fukuoka, Fukuoka 812-8582

1E-mail: omurat{at}mxs.meshnet.or.jp

The intracellular sorting of newly synthesized precursor proteins (preproteins) to mitochondria depends on the "mitochondria-targeting sequence" (MTS), which is located at the amino termini of the preproteins. MTS is required, however, not only for targeting newly synthesized preproteins to mitochondria, but also for all the following steps along the mitochondrial protein import pathway. MTS of nascent preproteins is first recognized by a cytoplasmic molecular chaperone, MSF, and then by Tom70 and Tom20 of the mitochondrial outer membrane receptor complex, Tom5 and Tom40 of the outer membrane protein translocation machinery, Tim23 of the inner membrane protein translocation machinery, and finally the processing peptidase, MPP, in the matrix. MTS is a multi-role sorting sequence which specifically interacts with various components along the mitochondrial protein import pathway. Recognition of MTS at multiple steps during the import of preproteins may contribute to the strict sorting of proteins destined for mitochondria.


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