Purification of the inducible alpha-agglutinin of S. cerevisiae and molecular cloning of the gene.
The alpha-agglutinin responsible for mating type-specific agglutination of S. cerevisiae alpha-cells has been purified to homogeneity. The glycoprotein released from the cell surface under mild conditions has a relative molecular mass of 200 to 300 kDa as determined by SDS-gel electrophoresis. The protein moiety corresponds to 68.2 kDa. With an oligonucleotide corresponding to the N-terminal amino acid sequence, the alpha-agglutinin gene has been cloned and sequenced. From the DNA sequence, a protein of 631 amino acids with 12 potential N-glycosylation sites is predicted. The carboxy terminal one-third of the protein is not required for agglutination activity.
Hauser
K
K
Lehrstuhl für Zellbiologie und Pflanzenphysiologie, Universität Regensburg, FRG.
Tanner
W
W
D000371:Agglutination; D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D005800:Genes, Fungal; D000072235:Mating Factor; D008969:Molecular Sequence Data; D010452:Peptide Biosynthesis; D010455:Peptides / Q000235:genetics / Q000302:isolation & purification*; D010675:Pheromones / Q000302:isolation & purification; D012441:Saccharomyces cerevisiae / Q000235:genetics* / Q000502:physiology
D010455:Peptides; D010675:Pheromones; D000072235:Mating Factor