Details
| Original language | English |
|---|---|
| Pages (from-to) | 271-281 |
| Number of pages | 11 |
| Journal | Plant Molecular Biology |
| Volume | 25 |
| Issue number | 2 |
| Publication status | Published - 1 May 1994 |
| Externally published | Yes |
Abstract
The mitochondrial iron-sulfur protein (also termed Rieske iron-sulfur protein) of cytochrome c reductase was purified from potato tubers and identified with heterologous antibodies. The sequences of the N-terminus of this 25 kDa protein and of an internal peptide were determined to design oligonucleotide mixtures for screening a cDNA library. One class of cDNA clones containing an open reading frame of 265 amino acids was isolated. The encoded protein contains the peptide sequences of the 25 kDa protein and shares about 50% sequence identity with the Rieske iron-sulfur proteins from fungi and around 43% with those from mammals. In vitro transcription and translation of the cDNA reveals that the iron-sulfur protein is made as a larger precursor of 30 kDa which is processed by the cytochrome c reductase/processing peptidase complex from potato. The processing product obtained after in vitro processing has the same size as the mature protein imported into isolated mitochondria. The presequence, which targets the protein to the organelle, is 53 amino acids long and has molecular features different from those found in presequences of fungal iron-sulfur proteins, which are processed in two steps. Our results indicate that, unlike in yeast and Neurospora, the presequence of the iron-sulfur protein from potato is removed by a single processing enzyme in one step.
Keywords
- cytochrome c reductase, mitochondria, potato, protein import, Rieske iron-sulfur protein
ASJC Scopus subject areas
- Agricultural and Biological Sciences(all)
- Agronomy and Crop Science
- Biochemistry, Genetics and Molecular Biology(all)
- Genetics
- Agricultural and Biological Sciences(all)
- Plant Science
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In: Plant Molecular Biology, Vol. 25, No. 2, 01.05.1994, p. 271-281.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Molecular features, processing and import of the Rieske iron-sulfur protein from potato mitochondria
AU - Emmermann, Michael
AU - Clericus, Monika
AU - Braun, Hans-Peter
AU - Mozo, Teresa
AU - Heins, Lisa
AU - Kruft, Volker
AU - Schmitz, Udo
PY - 1994/5/1
Y1 - 1994/5/1
N2 - The mitochondrial iron-sulfur protein (also termed Rieske iron-sulfur protein) of cytochrome c reductase was purified from potato tubers and identified with heterologous antibodies. The sequences of the N-terminus of this 25 kDa protein and of an internal peptide were determined to design oligonucleotide mixtures for screening a cDNA library. One class of cDNA clones containing an open reading frame of 265 amino acids was isolated. The encoded protein contains the peptide sequences of the 25 kDa protein and shares about 50% sequence identity with the Rieske iron-sulfur proteins from fungi and around 43% with those from mammals. In vitro transcription and translation of the cDNA reveals that the iron-sulfur protein is made as a larger precursor of 30 kDa which is processed by the cytochrome c reductase/processing peptidase complex from potato. The processing product obtained after in vitro processing has the same size as the mature protein imported into isolated mitochondria. The presequence, which targets the protein to the organelle, is 53 amino acids long and has molecular features different from those found in presequences of fungal iron-sulfur proteins, which are processed in two steps. Our results indicate that, unlike in yeast and Neurospora, the presequence of the iron-sulfur protein from potato is removed by a single processing enzyme in one step.
AB - The mitochondrial iron-sulfur protein (also termed Rieske iron-sulfur protein) of cytochrome c reductase was purified from potato tubers and identified with heterologous antibodies. The sequences of the N-terminus of this 25 kDa protein and of an internal peptide were determined to design oligonucleotide mixtures for screening a cDNA library. One class of cDNA clones containing an open reading frame of 265 amino acids was isolated. The encoded protein contains the peptide sequences of the 25 kDa protein and shares about 50% sequence identity with the Rieske iron-sulfur proteins from fungi and around 43% with those from mammals. In vitro transcription and translation of the cDNA reveals that the iron-sulfur protein is made as a larger precursor of 30 kDa which is processed by the cytochrome c reductase/processing peptidase complex from potato. The processing product obtained after in vitro processing has the same size as the mature protein imported into isolated mitochondria. The presequence, which targets the protein to the organelle, is 53 amino acids long and has molecular features different from those found in presequences of fungal iron-sulfur proteins, which are processed in two steps. Our results indicate that, unlike in yeast and Neurospora, the presequence of the iron-sulfur protein from potato is removed by a single processing enzyme in one step.
KW - cytochrome c reductase
KW - mitochondria
KW - potato
KW - protein import
KW - Rieske iron-sulfur protein
UR - http://www.scopus.com/inward/record.url?scp=0028429953&partnerID=8YFLogxK
U2 - 10.1007/BF00023243
DO - 10.1007/BF00023243
M3 - Article
C2 - 8018875
AN - SCOPUS:0028429953
VL - 25
SP - 271
EP - 281
JO - Plant Molecular Biology
JF - Plant Molecular Biology
SN - 0167-4412
IS - 2
ER -