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. 1986 Jan;5(1):161–165. doi: 10.1002/j.1460-2075.1986.tb04191.x

Intracellular sorting of alcohol dehydrogenase isoenzymes in yeast: a cytosolic location reflects absence of an amino-terminal targeting sequence for the mitochondrion.

A P van Loon, E T Young
PMCID: PMC1166709  PMID: 2937632

Abstract

The yeast Saccharomyces cerevisiae contains three alcohol dehydrogenase isoenzymes (ADHI-ADHIII), two in the cytoplasm (ADHI and ADHII) and one in the mitochondrion (ADHIII). Sequence comparison of the corresponding nuclear genes showed that these three proteins are 80-90% identical except for a 27-amino acid extension at the amino terminus of ADHIII. Here we demonstrate that ADHIII is located inside the mitochondrial inner membrane. We also show, using gene fusions, that the amino terminus of ADHIII contains the information for targeting the protein to and transporting it into the mitochondrion. The mitochondrial isoenzyme ADHIII can be converted into a cytosolic protein by deleting its first 28 amino acids. Conversely, the cytoplasmic isoenzyme ADHII can be converted into a mitochondrial isoenzyme by replacing its first 21 amino acids with the first 48 amino acids of ADHIII. We conclude that ADHII is a cytosolic protein because it lacks an amino-terminal targeting sequence for the mitochondrion and that ADHIII is a mitochondrial protein because it contains a mitochondrial targeting sequence.

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Selected References

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