Purification and amino acid sequence of mating factor from Saccharomyces cerevisiae

J Biochem. 1977 Dec;82(6):1681-7. doi: 10.1093/oxfordjournals.jbchem.a131864.

Abstract

Mating factor is a peptide excreted into the culture fluid by alpha-mating type cells of Saccharomyces cerevisiae X-2180 1B. The purification of the mating factor was carried out by ion exchange chromatography on phosphocellulose and Amberlite IRC 50 columns, followed by gel filtration on a Sephadex LH 20 column. The factor thus prepared was a peptide composed of Lys1, His1, Trp2, Gln2, Pro2, Gly1, Met1, Leu2 and Tyr1, and was able to induce morphological changes on alpha-mating type cells at a concentration of 5 pg/ml. The amino acid sequence of the mating factor was determined by the manual Edman degradation method using intact mating factor and its thermolytic peptides. The C-terminal amino acid residue was determined by digesting the factor with carboxypeptidase A. The complete amino acid sequence of the mating factor was established to be as follows: Trp-His-Trp-Leu-Gln-Leu-Lys-Pro-Gly-Gln-Pro-Met-Tyr.

MeSH terms

  • Amino Acid Sequence
  • Peptide Fragments / analysis
  • Peptides* / isolation & purification
  • Peptides* / physiology
  • Saccharomyces cerevisiae / physiology*
  • Spectrophotometry, Ultraviolet

Substances

  • Peptide Fragments
  • Peptides