NH2-terminal sequence of the isolated yeast ATP synthase subunit 6 reveals post-translational cleavage.
The three mitochondrially translated ATP synthase subunits of Saccharomyces cerevisiae were extracted from the enzyme and from whole mitochondria using an organic solvent mixture and then purified by reverse-phase HPLC. The amino acid composition of subunit 6 is close to the one predicted from the oli2 gene. The partial amino terminal sequence of subunit 6 reveals a post-translational cleavage site between the Thr-10 and Ser-11 residues of the precursor. Thus, mature subunit 6 contains 249 amino acid residues and displays a molecular mass of 27943 Da.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000302:isolation & purification*; D005796:Genes; D008928:Mitochondria / Q000201:enzymology; D010455:Peptides / Q000302:isolation & purification; D011499:Protein Processing, Post-Translational; D006180:Proton-Translocating ATPases / Q000032:analysis*; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000235:genetics
D000596:Amino Acids; D010455:Peptides; D006180:Proton-Translocating ATPases