The 'Hinge' protein of cytochrome c reductase from potato lacks the acidic domain and has no cleavable presequence.
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.
Institut für Genbiologische Forschung GmbH, Berlin, Germany.
H P
HP
Braun
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L
Jänsch
V
V
Kurft
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UK
Schmitz
D000595:Amino Acid Sequence; D001483:Base Sequence; D018076:DNA, Complementary / Q000235:genetics; D015723:Gene Library; D008928:Mitochondria / Q000201:enzymology*; D008969:Molecular Sequence Data; D009245:NADH Dehydrogenase / Q000737:chemistry / Q000235:genetics*; D011487:Protein Conformation; D011499:Protein Processing, Post-Translational; D021382:Protein Sorting Signals; D011506:Proteins / Q000737:chemistry / Q000235:genetics*; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid; D011198:Solanum tuberosum / Q000201:enzymology / Q000235:genetics*
D018076:DNA, Complementary; D021382:Protein Sorting Signals; D011506:Proteins; D009245:NADH Dehydrogenase