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J Biol Chem, Vol. 273, Issue 47, 31097-31102, November 20, 1998
From the Department of Chemistry, Faculty of Science, Kyushu
University, Fukuoka 812-8581, Japan
Outer mitochondrial membrane cytochrome
b5 (OMb), which is an isoform of cytochrome
b5 (cyt b5) in the
endoplasmic reticulum, is a typical tail-anchored protein of the outer
mitochondrial membrane. We cloned cDNA containing the complete
amino acid sequence of OMb and found that the protein has no typical
structural feature common to the mitochondrial targeting signal at the
amino terminus. To identify the region responsible for the
mitochondrial targeting of OMb, various mutated proteins were expressed
in cultured mammalian cells, and the subcellular localization of the
expressed proteins was analyzed. The deletion of more than 11 amino
acid residues from the carboxyl-terminal end of OMb abolished the
targeting of the protein to the mitochondria. When the
carboxyl-terminal 10 amino acids of OMb were fused to the cyt
b5 that was previously deleted in the
corresponding 10 residues, the fused protein localized in the
mitochondria, thereby indicating that the carboxyl-terminal 10 amino
acid residues of OMb have sufficient information to transport OMb to
the mitochondria. The replacement of either of the two positively
charged residues within the carboxyl-terminal 10 amino acids by alanine
resulted in the transport of the mutant proteins to the endoplasmic
reticulum. The mutant cyt b5, in which the acidic amino acid in its carboxyl-terminal end was replaced by basic
amino acid, could be transported to the mitochondria. It would thus
seem that charged amino acids in the carboxyl-terminal portion of these
proteins determine their locations in the cell.
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