The nuclear-coded subunits of yeast cytochrome c oxidase. The amino acid sequences of subunits VII and VIIa, structural similarities between the three smallest polypeptides of the holoenzyme, and implications for biogenesis

The complete amino acid sequences of subunits VII and VIIa from yeast cytochrome c oxidase are reported. Subunits VII and VIIa are 57 residues (Mr = 6603) and 54 residues (Mr = 6303) in length, respectively. Both polypeptides are amphiphilic, have an internal hydrophobic section and hydrophilic NH2...

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Bibliographic Details
Published in:The Journal of biological chemistry 1986-07, Vol.261 (20), p.9206-9209
Main Authors: Power, S D, Lochrie, M A, Poyton, R O
Format: Article
Language:English
Subjects:
ACTIVIDAD ENZIMATICA
ACTIVITE ENZYMATIQUE
Amino Acid Sequence
Biological and medical sciences
Cell structures and functions
Electron Transport Complex IV - biosynthesis
ENZYMIC ACTIVITY
Fundamental and applied biological sciences. Psychology
Mitochondria and cell respiration
Molecular and cellular biology
OXIDOREDUCTASES
OXIDORREDUCTASAS
OXYDOREDUCTASE
PEPTIDE
Peptide Fragments
PEPTIDES
PEPTIDOS
SACCHAROMYCES CEREVISIAE
Saccharomyces cerevisiae - enzymology
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Summary:The complete amino acid sequences of subunits VII and VIIa from yeast cytochrome c oxidase are reported. Subunits VII and VIIa are 57 residues (Mr = 6603) and 54 residues (Mr = 6303) in length, respectively. Both polypeptides are amphiphilic, have an internal hydrophobic section and hydrophilic NH2 and COOH termini, and terminate at their COOH termini with a basic amino acid. This structural motif is similar to that possessed by subunit VIII of yeast cytochrome c oxidase. All three polypeptides have hydrophobic sections which are long enough to span the inner membrane; all three polypeptides lack methionine at their NH2 termini; and all three polypeptides have COOH termini which could result from proteolysis by a protease with trypsin or cathepsin B-like activity. These observations raise the interesting possibility that subunits VII, VIIa, and VIII are transmembranous polypeptides which are processed at both their NH2 and COOH termini during their biogenesis.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(18)67640-9