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J. Biochem, 1989, Vol. 106, No. 1 181-187
© 1989 Japanese Biochemical Society

research-article

Protein Sorting between the Outer and Inner Mitochondrial Membranes: Submitochondrial Localization of Cytochrome cx Whose Presequence is Replaced by the Amino-Terminal Region of a 70 kDa Outer Membrane Protein1

Masato Nakai*, Masayuki Harabayashi*, Toshiharu Hase** and Hiroshi Matsubara*

*Department of Biology, Faculty of Science, Osaka University Toyonaka, Osaka 560
**Department of Agricultural Chemistry, School of Agriculture, Nagoya University Chikusa-ku, Nagoya, Aichi 464

The amino-terminal region of a 70 kDa mitochondrial outer membrane protein of yeast and the presequence of cytochrome c, an inner membrane protein exposed to the intermem-brane space, are thought to be responsible for localizing the proteins in their final destinations after synthesis in the cytosol. Gene fusion experiments were used to identify signals that are responsible for protein sorting between the outer and inner mitochondrial membranes. The submitochondrial localization of cytochrome cx whose presequence was replaced by the amino-terminal region of the 70 kDa mitochondrial outer membrane protein has been investigated. We have also used an in vivo complementation assay to determine whether or not a 70k-cyt c1 fusion protein is functional. Both the first half and all of the presequence of cytochrome cx can be replaced by the amino-terminal 12 or 29 residues of the 70 kDa protein for transport to the inner membrane and functional assembly into succinate-cytochrome c reductase. However, replacements by the amino-terminal 61 residues of the 70 kDa protein result in exclusive localization of the fusion proteins to the outer membrane, and the fusions cannot be assembled into the enzyme complex. These data indicate that a mitochondrial targeting signal alone is sufficient to direct cytochrome cx of mature size to the inner membrane.

1This work was supported in part by a Grant-in-Aid for Scientific Research on the Priority Area of Bioenergetics and grant No. 62470148 from the Ministry of Education, Science and Culture of Japan.


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