Molecular Basis of Cell-Cell Recognition in Yeast
Abstract
The research objectives were to isolate and characterize the sexual agglutination factors from the two haploid cell types of the yeast Saccharomyces kluyveri, with the eventual goal of defining the precise molecular structures of the two agglutinins, thereby contributing to a better understanding of all types of cellular adhesion. The heat-labile sexual agglutinin from Saccharomyces kluyveri 17-cells was isolated and shown to consist of 3 domains, a glycopeptide part containing all of the N-linked oligo-saccharides and making up one-third of the protein that was embedded in the cell wall and held the agglutinin on the cell surface, a carbohydrate-free polypeptide portion of 60 kDa that possessed the recognizer site, and a glycopeptide with 0-linked carbohydrate that interconnected the other 2 domains. The heat-stable sexual agglutinin from S. kluyveri cells was isolated and shown to consist of a large glycopeptide making up 80% of the mass of the agglutinin that was anchored in the cell wall and a small glycopeptide of 25 kDa that had the site of recognition that interacted with the 60 kDa 17-cell fragment. The 25 kDa site was released from the intact molecule by reducing agents, which shows that it is attached by a disulfide bond, and partial sequence data and smaller proteolytic fragments have been obtained. These results demonstrate that the sexual agglutination reaction in yeast has many similarities to the fertilization reaction in higher eucaryotes. Keywords: Yeast cell wall; Saccharomyces kouyveri; Sexual agglutination; Mannoprotein; Proteolysis.
Document Details
- Document Type
- Technical Report
- Publication Date
- Jun 29, 1988
- Accession Number
- ADA197031
Entities
People
- Clinton E. Ballou
Organizations
- University of California, Berkeley