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The nuclear-coded subunits of yeast cyto ... and implications for biogenesis
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.
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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.
Power SD, Lochrie MA, Poyton RO
The Journal of biological chemistry
1986-07-15 00:00
261
20
9206-9
Amino Acid Sequence,Electron Transport Complex IV,Peptide Fragments,Saccharomyces cerevisiae,Peptide Fragments,Electron Transport Complex IV
J. Biol. Chem.
NIGMS GM 29838, NIGMS GM 30228
0021-9258
1071
True
3013877
