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. 1992 Sep;11(9):3219–3227. doi: 10.1002/j.1460-2075.1992.tb05399.x

The general mitochondrial processing peptidase from potato is an integral part of cytochrome c reductase of the respiratory chain.

H P Braun 1, M Emmermann 1, V Kruft 1, U K Schmitz 1
PMCID: PMC556855  PMID: 1324169

Abstract

The major mitochondrial processing activity removing presequences from nuclear encoded precursor proteins is present in the soluble fraction of fungal and mammalian mitochondria. We found that in potato, this activity resides in the inner mitochondrial membrane. Surprisingly, the proteolytic activity co-purifies with cytochrome c reductase, a protein complex of the respiratory chain. The purified complex is bifunctional, as it has the ability to transfer electrons from ubiquinol to cytochrome c and to cleave off the presequences of mitochondrial precursor proteins. In contrast to the nine subunit fungal complex, cytochrome c reductase from potato comprises 10 polypeptides. Protein sequencing of peptides from individual subunits and analysis of corresponding cDNA clones reveals that subunit III of cytochrome c reductase (51 kDa) represents the general mitochondrial processing peptidase.

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