Details
| Original language | English |
|---|---|
| Pages (from-to) | 90-94 |
| Number of pages | 5 |
| Journal | FEBS letters |
| Volume | 347 |
| Issue number | 1 |
| Publication status | Published - 20 Jun 1994 |
| Externally published | Yes |
Abstract
The 'Hinge' protein of cytochrome c reductase from fungi and mammals is thought to support electron transport from cytochrome c1 to cytochrome c and was reported to be one of the most acidic proteins known. Isolation and analysis of cDNA clones of the first 'Hinge' protein from a plant source reveals that it has a surplus of basic residues in potato. While the overall identity between the deduced amino acid sequence of the potato 'Hinge' protein and the proteins from yeast and bovine is in the range of 40%, the characteristic acidic domain is lacking. Therefore the numerous theories on the function of the mitochondrial 'Hinge' protein seem not to apply for the protein from potato. Also the atypical acidic presequence of the 'Hinge' protein from fungi and mammals is absent as revealed by N-terminal sequencing of the isolated potato 'Hinge' protein. Functional implications of these results for the 'Hinge' proteins from other organisms are discussed.
Keywords
- 'Hinge' protein, Cytochrome c reductase, Mitochondrion, Protein import, Respiratory chain, Solanum tuberosum
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biophysics
- Biochemistry, Genetics and Molecular Biology(all)
- Structural Biology
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biochemistry, Genetics and Molecular Biology(all)
- Molecular Biology
- Biochemistry, Genetics and Molecular Biology(all)
- Genetics
- Biochemistry, Genetics and Molecular Biology(all)
- Cell Biology
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In: FEBS letters, Vol. 347, No. 1, 20.06.1994, p. 90-94.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - The 'Hinge' protein of cytochrome c reductase from potato lacks the acidic domain and has no cleavable presequence
AU - Braun, Hans Peter
AU - Jänsch, Lothar
AU - Kruft, Volker
AU - Schmitza, Udo K.
N1 - Funding information: assistance. This work was supported by the Deutsche Forschungsge-meinsehaft, Grant Schm. 698/2.
PY - 1994/6/20
Y1 - 1994/6/20
N2 - The 'Hinge' protein of cytochrome c reductase from fungi and mammals is thought to support electron transport from cytochrome c1 to cytochrome c and was reported to be one of the most acidic proteins known. Isolation and analysis of cDNA clones of the first 'Hinge' protein from a plant source reveals that it has a surplus of basic residues in potato. While the overall identity between the deduced amino acid sequence of the potato 'Hinge' protein and the proteins from yeast and bovine is in the range of 40%, the characteristic acidic domain is lacking. Therefore the numerous theories on the function of the mitochondrial 'Hinge' protein seem not to apply for the protein from potato. Also the atypical acidic presequence of the 'Hinge' protein from fungi and mammals is absent as revealed by N-terminal sequencing of the isolated potato 'Hinge' protein. Functional implications of these results for the 'Hinge' proteins from other organisms are discussed.
AB - The 'Hinge' protein of cytochrome c reductase from fungi and mammals is thought to support electron transport from cytochrome c1 to cytochrome c and was reported to be one of the most acidic proteins known. Isolation and analysis of cDNA clones of the first 'Hinge' protein from a plant source reveals that it has a surplus of basic residues in potato. While the overall identity between the deduced amino acid sequence of the potato 'Hinge' protein and the proteins from yeast and bovine is in the range of 40%, the characteristic acidic domain is lacking. Therefore the numerous theories on the function of the mitochondrial 'Hinge' protein seem not to apply for the protein from potato. Also the atypical acidic presequence of the 'Hinge' protein from fungi and mammals is absent as revealed by N-terminal sequencing of the isolated potato 'Hinge' protein. Functional implications of these results for the 'Hinge' proteins from other organisms are discussed.
KW - 'Hinge' protein
KW - Cytochrome c reductase
KW - Mitochondrion
KW - Protein import
KW - Respiratory chain
KW - Solanum tuberosum
UR - http://www.scopus.com/inward/record.url?scp=0028290026&partnerID=8YFLogxK
U2 - 10.1016/0014-5793(94)00515-X
DO - 10.1016/0014-5793(94)00515-X
M3 - Article
C2 - 8013669
AN - SCOPUS:0028290026
VL - 347
SP - 90
EP - 94
JO - FEBS letters
JF - FEBS letters
SN - 0014-5793
IS - 1
ER -