Chemical synthesis of the M-factor mating pheromone from Schizosaccharomyces pombe.
Conjugation in the fission yeast Schizosaccharomyces pombe is controlled by the reciprocal action of mating pheromones. We recently showed that M-factor, the pheromone released by cells of the cellular mating type Minus, is a nonapeptide in which the C-terminal cysteine residue is carboxyl-methylated and S-alkylated, probably with a farnesyl residue (Davey, 1992): Tyr-Thr-Pro-Lys-Val-Pro-Tyr-Met-Cys(S-farnesyl)- OCH3. Here we describe the chemical synthesis of this modified peptide and show that it exhibits all of the properties of the native pheromone. These results confirm the structure of the M-factor while the production of relatively large amounts of pure pheromone will be invaluable for studying the mating response in this yeast.
Wang
S H
SH
Department of Chemistry, College of Staten Island, City University of New York 10314.
Xue
C B
CB
Nielsen
O
O
Davey
J
J
Naider
F
F
D000595:Amino Acid Sequence; D004268:DNA-Binding Proteins; D036341:Intercellular Signaling Peptides and Proteins; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis*; D010675:Pheromones / Q000138:chemical synthesis*; D012568:Schizosaccharomyces / Q000737:chemistry* / Q000254:growth & development; D029702:Schizosaccharomyces pombe Proteins
D004268:DNA-Binding Proteins; D036341:Intercellular Signaling Peptides and Proteins; C089516:Mating Factor, S pombe; D010455:Peptides; D010675:Pheromones; D029702:Schizosaccharomyces pombe Proteins; C490320:mfm1 protein, S pombe