NH2-terminal sequence of the isolated yeast ATP synthase subunit 6 reveals post-translational cleavage

Eur J Biochem. 1988 Mar 15;172(3):621-5. doi: 10.1111/j.1432-1033.1988.tb13934.x.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / isolation & purification*
  • Genes
  • Mitochondria / enzymology
  • Peptides / isolation & purification
  • Protein Processing, Post-Translational*
  • Proton-Translocating ATPases / analysis*
  • Saccharomyces cerevisiae / enzymology*
  • Saccharomyces cerevisiae / genetics

Substances

  • Amino Acids
  • Peptides
  • Proton-Translocating ATPases