MATING TYPE-SPECIFIC CELL-CELL RECOGNITION OF SACCHAROMYCES-CEREVISIAE - CELL-WALL ATTACHMENT AND ACTIVE-SITES OF A-AGGLUTININ AND ALPHA-AGGLUTININ

CAPPELLARO, C and BALDERMANN, C and RACHEL, R and TANNER, W (1994) MATING TYPE-SPECIFIC CELL-CELL RECOGNITION OF SACCHAROMYCES-CEREVISIAE - CELL-WALL ATTACHMENT AND ACTIVE-SITES OF A-AGGLUTININ AND ALPHA-AGGLUTININ. EMBO JOURNAL, 13 (20). pp. 4737-4744. ISSN 0261-4189,

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Abstract

Mating type-specific agglutination of Saccharomyces cerevisiae a and alpha cells depends on the heterophilic interaction of two cell surface glycoproteins, the gene products of AG alpha 1 and AGA2. Evidence is presented with immunogold labelling that the alpha-agglutinin is part of the outer fimbrial cell wall coat. The a-agglutinin is bound via two S-S bridges (Cys7 and Cys50) to a cell wall component, most probably the gene product of AGA1. His273 of alpha-agglutinin has previously been shown to be essential for a- and alpha-agglutinin interaction and a model based on two opposing ion-pairs had been proposed. By site-directed mutagenesis this possibility has now been excluded. With the help of various peptides, either chemically synthesized, obtained by proteolysis of intact glycosylated a-agglutinin or prepared from a fusion protein expressed in Escherichia coli, the biologically active region of a-agglutinin was located at the C-terminus of the molecule. A peptide consisting of the C-terminal 10 amino acids (GSPIN-TQYVF) was active in nanomolar concentrations. Saccharide moieties, therefore, are not essential for the mating type-specific cell-cell interaction; glycosylated peptides are, however, four to five times more active than non-glycosylated ones. Comparisons of the recognition sequences of the S.cerevisiae agglutinins with that of the Dictyostelium contact site A glycoprotein (gp80), as well as with those of the various families of eel adhesion molecules of higher eucaryotes, have been made and are discussed.

Item Type: Article
Uncontrolled Keywords: ADHESION MOLECULE; SEXUAL AGGLUTINATION; HOMOPHILIC BINDING; A-AGGLUTININ; GLYCOPROTEIN; IDENTIFICATION; PURIFICATION; CLONING; YEAST; SEQUENCE; AGGLUTININS; CELL RECOGNITION; GLYCOPROTEINS; SACCHAROMYCES-CEREVISIAE
Depositing User: Dr. Gernot Deinzer
Last Modified: 19 Oct 2022 08:39
URI: https://pred.uni-regensburg.de/id/eprint/53027

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