title: NH2-terminal sequence of the isolated yeast ATP synthase subunit 6 reveals post-translational cleavage.
abstract: 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.
mesh_terms: 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
chemical_list: D000596:Amino Acids; D010455:Peptides; D006180:Proton-Translocating ATPases