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Mol Cell Biol

Title:		"Cell surface anchorage and ligand-binding domains of the Saccharomyces cerevisiae cell adhesion protein alpha-agglutinin, a member of the immunoglobulin superfamily"
Author(s):		Wojciechowicz D; Lu CF; Kurjan J; Lipke PN;
Address:		"Department of Biological Sciences, Hunter College, City University of New York, New York 10021"
Journal Title:		Mol Cell Biol
Year:		1993
Volume:		13
Issue:		4
Page Number:		2554 - 2563
DOI:		10.1128/mcb.13.4.2554-2563.1993
ISSN/ISBN:		0270-7306 (Print) 1098-5549 (Electronic) 0270-7306 (Linking)
Abstract:		"alpha-Agglutinin is a cell adhesion glycoprotein expressed on the cell wall of Saccharomyces cerevisiae alpha cells. Binding of alpha-agglutinin to its ligand a-agglutinin, expressed by a cells, mediates cell-cell contact during mating. Analysis of truncations of the 650-amino-acid alpha-agglutinin structural gene AG alpha 1 delineated functional domains of alpha-agglutinin. Removal of the C-terminal hydrophobic sequence allowed efficient secretion of the protein and loss of cell surface attachment. This cell surface anchorage domain was necessary for linkage to a glycosyl phosphatidylinositol anchor. A construct expressing the N-terminal 350 amino acid residues retained full a-agglutinin-binding activity, localizing the binding domain to the N-terminal portion of alpha-agglutinin. A 278-residue N-terminal peptide was inactive; therefore, the binding domain includes residues between 278 and 350. The segment of alpha-agglutinin between amino acid residues 217 and 308 showed significant structural and sequence similarity to a consensus sequence for immunoglobulin superfamily variable-type domains. The similarity of the alpha-agglutinin-binding domain to mammalian cell adhesion proteins suggests that this structure is a highly conserved feature of adhesion proteins in diverse eukaryotes"
Keywords:		Amino Acid Sequence Binding Sites Cell Adhesion Molecules/*metabolism Cell Membrane/metabolism Consensus Sequence DNA Mutational Analysis Fungal Proteins/*metabolism Glycoproteins/metabolism Glycosylation Immunoglobulins/chemistry Inositol/metabolism Liga;
Notes:		"MedlineWojciechowicz, D Lu, C F Kurjan, J Lipke, P N eng Comparative Study Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. 1993/04/01 Mol Cell Biol. 1993 Apr; 13(4):2554-63. doi: 10.1128/mcb.13.4.2554-2563.1993"