Details
| Original language | English |
|---|---|
| Pages (from-to) | 237-245 |
| Number of pages | 9 |
| Journal | MGG Molecular & General Genetics |
| Volume | 245 |
| Issue number | 2 |
| Publication status | Published - Mar 1994 |
| Externally published | Yes |
Abstract
Cytochrome c reductase from potato is a bifunctional protein complex located in the inner mitochondrial membrane, which is involved in respiratory electron transport and processing of mitochondrial precursor proteins. The three largest subunits of the complex share the highest degree of sequence identity with the α- and β-subunits of the soluble processing peptidase (MPP) from fungi and mammals. Evidence is provided that another substoichiometric polypeptide of the cytochrome c reductase complex resembles the α-subunit of MPP. A cDNA clone corresponding to the second α-MPP protein (α-II MPP) encodes a polypeptide of 504 amino acids which is 84% identical to α-I MPP. The two different a-MPP polypeptides have similar sizes on SDS-polyacrylamide gels but can be distinguished with an antibody raised against a decapeptide that is specific for a-II MPP. The presequences of both α-subunits of MPP are proteolytically removed by the integrated processing enzyme complex indicating that it acts on the targeting signals of its own precursor proteins. Gene-specific oligonucleotides reveal that the genes encoding a-subunit I and α-subunit II of MPP are differentially expressed in all tissues analysed but the transcript levels do not vary between tissues.
Keywords
- Cytochrome c reductase, Mitochondria, Potato, Processing peptidase, Protein import
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Genetics
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In: MGG Molecular & General Genetics, Vol. 245, No. 2, 03.1994, p. 237-245.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - The mitochondrial processing peptidase from potato
T2 - A self-processing enzyme encoded by two differentially expressed genes
AU - Emmermann, Michael
AU - Braun, Hans-Peter
AU - Schmitz, Udo
PY - 1994/3
Y1 - 1994/3
N2 - Cytochrome c reductase from potato is a bifunctional protein complex located in the inner mitochondrial membrane, which is involved in respiratory electron transport and processing of mitochondrial precursor proteins. The three largest subunits of the complex share the highest degree of sequence identity with the α- and β-subunits of the soluble processing peptidase (MPP) from fungi and mammals. Evidence is provided that another substoichiometric polypeptide of the cytochrome c reductase complex resembles the α-subunit of MPP. A cDNA clone corresponding to the second α-MPP protein (α-II MPP) encodes a polypeptide of 504 amino acids which is 84% identical to α-I MPP. The two different a-MPP polypeptides have similar sizes on SDS-polyacrylamide gels but can be distinguished with an antibody raised against a decapeptide that is specific for a-II MPP. The presequences of both α-subunits of MPP are proteolytically removed by the integrated processing enzyme complex indicating that it acts on the targeting signals of its own precursor proteins. Gene-specific oligonucleotides reveal that the genes encoding a-subunit I and α-subunit II of MPP are differentially expressed in all tissues analysed but the transcript levels do not vary between tissues.
AB - Cytochrome c reductase from potato is a bifunctional protein complex located in the inner mitochondrial membrane, which is involved in respiratory electron transport and processing of mitochondrial precursor proteins. The three largest subunits of the complex share the highest degree of sequence identity with the α- and β-subunits of the soluble processing peptidase (MPP) from fungi and mammals. Evidence is provided that another substoichiometric polypeptide of the cytochrome c reductase complex resembles the α-subunit of MPP. A cDNA clone corresponding to the second α-MPP protein (α-II MPP) encodes a polypeptide of 504 amino acids which is 84% identical to α-I MPP. The two different a-MPP polypeptides have similar sizes on SDS-polyacrylamide gels but can be distinguished with an antibody raised against a decapeptide that is specific for a-II MPP. The presequences of both α-subunits of MPP are proteolytically removed by the integrated processing enzyme complex indicating that it acts on the targeting signals of its own precursor proteins. Gene-specific oligonucleotides reveal that the genes encoding a-subunit I and α-subunit II of MPP are differentially expressed in all tissues analysed but the transcript levels do not vary between tissues.
KW - Cytochrome c reductase
KW - Mitochondria
KW - Potato
KW - Processing peptidase
KW - Protein import
UR - http://www.scopus.com/inward/record.url?scp=0028072873&partnerID=8YFLogxK
U2 - 10.1007/BF00283272
DO - 10.1007/BF00283272
M3 - Article
C2 - 7816032
AN - SCOPUS:0028072873
VL - 245
SP - 237
EP - 245
JO - MGG Molecular & General Genetics
JF - MGG Molecular & General Genetics
SN - 0026-8925
IS - 2
ER -