Details
| Original language | English |
|---|---|
| Pages (from-to) | 3219-3227 |
| Number of pages | 9 |
| Journal | EMBO Journal |
| Volume | 11 |
| Issue number | 9 |
| Publication status | Published - 1992 |
| Externally published | Yes |
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.
Keywords
- Cytochrome c reductese, Mitochondria, Potato, Processing peptidase, Protein import
ASJC Scopus subject areas
- Neuroscience(all)
- Biochemistry, Genetics and Molecular Biology(all)
- Molecular Biology
- Biochemistry, Genetics and Molecular Biology(all)
- Immunology and Microbiology(all)
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In: EMBO Journal, Vol. 11, No. 9, 1992, p. 3219-3227.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - The general mitochondrial processing peptidase from potato is an integral part of cytochrome c reductase of the respiratory chain
AU - Braun, Hans-Peter
AU - Emmermann, Michael
AU - Kruft, Volker
AU - Schmitz, Udo
PY - 1992
Y1 - 1992
N2 - 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.
AB - 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.
KW - Cytochrome c reductese
KW - Mitochondria
KW - Potato
KW - Processing peptidase
KW - Protein import
UR - http://www.scopus.com/inward/record.url?scp=0026709336&partnerID=8YFLogxK
M3 - Article
C2 - 1324169
AN - SCOPUS:0026709336
VL - 11
SP - 3219
EP - 3227
JO - EMBO Journal
JF - EMBO Journal
SN - 0261-4189
IS - 9
ER -