Cytochrome c from Schizosaccharomyces pombe

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Abstract
The amino acid sequence of S. pombe cytochrome c was established by automatic degradation of the protein and by manual degradation of fragments obtained by cyanogen bromide cleavage and chymotryptic digestion. The chymotryptic peptides were aligned by homology with other known cytochrome c sequences. The protein in 108 residues long, with a 4-residue amino-terminal tail. It has only 1 methionine residue and differs from other fungal cytochromes c in lacking the 1-residue deletion at the C-terminal end. After a cyanogen bromide step, an unexpected cleavage of the peptide chain before a cysteine residue was boserved. This is ascribed to formation of a dehydroalanyl residue during an incomplete S-carboxymethylation of the apoprotein, and subsequent cleavage under acidic conditions. Experimental evidence is presented in favor of the proposed mechanisms.

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