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Mol Cell Biol

Title:		"AG alpha 1 is the structural gene for the Saccharomyces cerevisiae alpha-agglutinin, a cell surface glycoprotein involved in cell-cell interactions during mating"
Author(s):		Lipke PN; Wojciechowicz D; Kurjan J;
Address:		"Department of Biological Sciences, Hunter College of the City University of New York, New York 10021"
Journal Title:		Mol Cell Biol
Year:		1989
Volume:		9
Issue:		8
Page Number:		3155 - 3165
DOI:		10.1128/mcb.9.8.3155-3165.1989
ISSN/ISBN:		0270-7306 (Print) 1098-5549 (Electronic) 0270-7306 (Linking)
Abstract:		"We have cloned the alpha-agglutinin structural gene, AG alpha 1, by the isolation of alpha-specific agglutination-defective mutants, followed by isolation of a complementing plasmid. Independently isolated alpha-specific agglutination-defective mutations were in a single complementation group, consistent with biochemical results indicating that the alpha-agglutinin is composed of a single polypeptide. Mapping results suggested that the complementation group identified by these mutants is allelic to the ag alpha 1 mutation identified previously. Expression of AG alpha 1 RNA was alpha specific and inducible by a-factor. Sequences similar to the consensus sequences for positive control by MAT alpha 1 and pheromone induction were found upstream of the AG alpha 1 initiation codon. The AG alpha 1 gene could encode a 650-amino-acid protein with a putative signal sequence, 12 possible N-glycosylation sites, and a high proportion of serine and threonine residues, all of which are features expected for the alpha-agglutinin sequence. Disruption of the AG alpha 1 gene resulted in failure to express alpha-agglutinin and loss of cellular agglutinability in alpha cells. An Escherichia coli fusion protein containing 229 amino acids of the AG alpha 1 sequence was recognized by an anti-alpha-agglutinin antibody. In addition, the ability of this antibody to inhibit agglutination was prevented by this fusion protein. These results indicate that AG alpha 1 encodes alpha-agglutinin. Features of the AG alpha 1 gene product suggest that the amino-terminal half of the protein contains the a-agglutinin binding domain and that the carboxy-terminal half contains a cell surface localization domain, possibly including a glycosyl phosphatidylinositol anchor"
Keywords:		"Agglutinins/*genetics Amino Acid Sequence Amino Acids/analysis Base Sequence Blotting, Western Gene Expression Regulation *Genes *Genes, Fungal Genetic Complementation Test Genetic Vectors Mating Factor Membrane Glycoproteins/*genetics Molecular Sequence;"
Notes:		"MedlineLipke, P N Wojciechowicz, D Kurjan, J eng 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. 1989/08/01 Mol Cell Biol. 1989 Aug; 9(8):3155-65. doi: 10.1128/mcb.9.8.3155-3165.1989"