Details
| Original language | English |
|---|---|
| Pages (from-to) | 367-372 |
| Number of pages | 6 |
| Journal | BBA - Bioenergetics |
| Volume | 1188 |
| Issue number | 3 |
| Publication status | Published - 30 Dec 1994 |
| Externally published | Yes |
Abstract
Cytochrome c reductase from potato comprises ten subunits with apparent molecular sizes between 55 and < 10 kDa. The subunit with the highest electrophoretic mobility on SDS-polyacrylamide gels was isolated and analysed by cyclic Edman degradation. Mixtures of degenerative oligonuleotides were derived from the obtained sequence data and used for the isolation of corresponding cDNA clones. The clones encode a protein of 72 amino acids which exhibits significant sequence identity with a 9.5 kDa subunit of cytochrome c reductase from bovine and a 11 kDa subunit of the enzyme complex from yeast. Comparison between the deduced amino acid sequence of the open reading frame and the sequence of the mature protein reveals that only the initiator methionine is absent in the functional subunit. Hence the protein has a calculated molecular mass of 8.2 kDa. Transcripts of the potato 8.2 kDa protein were not translated in reticulocyte lysates but in vitro translation worked efficiently with wheat germ lysate. Import of the radiolabelled protein into isolated mitochondria from potato seems to depend on a potential across the inner membrane and confirms the absence of a cleavable mitochondrial presequence.
Keywords
- (S. tuberosum), Cytochrome bc complex, Cytochrome c reductase, Mitochondrion, Protein transport, Respiratory chain
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biophysics
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biochemistry, Genetics and Molecular Biology(all)
- Cell Biology
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In: BBA - Bioenergetics, Vol. 1188, No. 3, 30.12.1994, p. 367-372.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Primary structure, cell-free synthesis and mitochondrial targeting of the 8.2 kDa protein of cytochrome c reductase from potato
AU - Braun, Hans-Peter
AU - Kruft, Volker
AU - Schmitz, Udo
N1 - Funding information: We wish to thank H. Mentzel for excellent technical assistance. This work was supported by the Deutsche Forschungsgemeinschaft, grant Schm. 698/2, and by the BMFT.
PY - 1994/12/30
Y1 - 1994/12/30
N2 - Cytochrome c reductase from potato comprises ten subunits with apparent molecular sizes between 55 and < 10 kDa. The subunit with the highest electrophoretic mobility on SDS-polyacrylamide gels was isolated and analysed by cyclic Edman degradation. Mixtures of degenerative oligonuleotides were derived from the obtained sequence data and used for the isolation of corresponding cDNA clones. The clones encode a protein of 72 amino acids which exhibits significant sequence identity with a 9.5 kDa subunit of cytochrome c reductase from bovine and a 11 kDa subunit of the enzyme complex from yeast. Comparison between the deduced amino acid sequence of the open reading frame and the sequence of the mature protein reveals that only the initiator methionine is absent in the functional subunit. Hence the protein has a calculated molecular mass of 8.2 kDa. Transcripts of the potato 8.2 kDa protein were not translated in reticulocyte lysates but in vitro translation worked efficiently with wheat germ lysate. Import of the radiolabelled protein into isolated mitochondria from potato seems to depend on a potential across the inner membrane and confirms the absence of a cleavable mitochondrial presequence.
AB - Cytochrome c reductase from potato comprises ten subunits with apparent molecular sizes between 55 and < 10 kDa. The subunit with the highest electrophoretic mobility on SDS-polyacrylamide gels was isolated and analysed by cyclic Edman degradation. Mixtures of degenerative oligonuleotides were derived from the obtained sequence data and used for the isolation of corresponding cDNA clones. The clones encode a protein of 72 amino acids which exhibits significant sequence identity with a 9.5 kDa subunit of cytochrome c reductase from bovine and a 11 kDa subunit of the enzyme complex from yeast. Comparison between the deduced amino acid sequence of the open reading frame and the sequence of the mature protein reveals that only the initiator methionine is absent in the functional subunit. Hence the protein has a calculated molecular mass of 8.2 kDa. Transcripts of the potato 8.2 kDa protein were not translated in reticulocyte lysates but in vitro translation worked efficiently with wheat germ lysate. Import of the radiolabelled protein into isolated mitochondria from potato seems to depend on a potential across the inner membrane and confirms the absence of a cleavable mitochondrial presequence.
KW - (S. tuberosum)
KW - Cytochrome bc complex
KW - Cytochrome c reductase
KW - Mitochondrion
KW - Protein transport
KW - Respiratory chain
UR - http://www.scopus.com/inward/record.url?scp=0028598297&partnerID=8YFLogxK
U2 - 10.1016/0005-2728(94)90057-4
DO - 10.1016/0005-2728(94)90057-4
M3 - Article
C2 - 7803451
AN - SCOPUS:0028598297
VL - 1188
SP - 367
EP - 372
JO - BBA - Bioenergetics
JF - BBA - Bioenergetics
SN - 0005-2728
IS - 3
ER -