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EMBO J

Title:		Mating type-specific cell-cell recognition of Saccharomyces cerevisiae: cell wall attachment and active sites of a- and alpha-agglutinin
Author(s):		Cappellaro C; Baldermann C; Rachel R; Tanner W;
Address:		"Lehrstuhl fur Zellbiologie und Pflanzenphysiologie, Universitat Regensburg, Germany"
Journal Title:		EMBO J
Year:		1994
Volume:		13
Issue:		20
Page Number:		4737 - 4744
DOI:		10.1002/j.1460-2075.1994.tb06799.x
ISSN/ISBN:		0261-4189 (Print) 1460-2075 (Electronic) 0261-4189 (Linking)
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 cell adhesion molecules of higher eucaryotes, have been made and are discussed"
Keywords:		"Agglutinins/genetics/metabolism/*physiology Amino Acid Sequence Base Sequence Binding Sites Cell Adhesion/*physiology Cell Adhesion Molecules Cell Wall/*metabolism Fungal Proteins/physiology Mating Factor Molecular Sequence Data Mutagenesis, Site-Directed;"
Notes:		"MedlineCappellaro, C Baldermann, C Rachel, R Tanner, W eng Research Support, Non-U.S. Gov't England 1994/10/17 EMBO J. 1994 Oct 17; 13(20):4737-44. doi: 10.1002/j.1460-2075.1994.tb06799.x"