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Genetics


Title:Conserved WCPL and CX4C domains mediate several mating adhesin interactions in Saccharomyces cerevisiae
Author(s):Huang G; Dougherty SD; Erdman SE;
Address:"Department of Biology, Syracuse University, Syracuse, New York 13244, USA"
Journal Title:Genetics
Year:2009
Volume:20090318
Issue:1
Page Number:173 - 189
DOI: 10.1534/genetics.108.100073
ISSN/ISBN:0016-6731 (Print) 0016-6731 (Linking)
Abstract:"Several adhesins are induced by pheromones during mating in Saccharomyces cerevisiae, including Aga1p, Aga2p, Sag1p (Agalpha1p), and Fig2p. These four proteins all participate in or influence a well-studied agglutinin interaction mediated by Aga1p-Aga2p complexes and Sag1p; however, they also play redundant and essential roles in mating via an unknown mechanism. Aga1p and Fig2p both contain repeated, conserved WCPL and CX(4)C domains. This study was directed toward understanding the mechanism underlying the collective requirement of agglutinins and Fig2p for mating. Apart from the well-known agglutinin interaction between Aga2p and Sag1p, three more pairs of interactions in cells of opposite mating type were revealed by this study, including bilateral heterotypic interactions between Aga1p and Fig2p and a homotypic interaction between Fig2p and Fig2p. These four pairs of adhesin interactions are collectively required for maximum mating efficiency and normal zygote morphogenesis. GPI-less, epitope-tagged forms of Aga1p and Fig2p can be co-immunoprecipitated from the culture medium of mating cells in a manner dependent on the WCPL and CX(4)C domains in the R1 repeat of Aga1p. Using site-directed mutagenesis, the conserved residues in Aga1p that interact with Fig2p were identified. Aga1p is involved in two distinct adhesive functions that are independent of each other, which raises the possibility for combinatorial interactions of this protein with its different adhesion receptors, Sag1 and Fig2p, a property of many higher eukaryotic adhesins"
Keywords:"Amino Acid Sequence Blotting, Western Cell Adhesion Molecules/genetics/*metabolism Immunoprecipitation Molecular Sequence Data Morphogenesis *Protein Interaction Domains and Motifs Protein Structure, Tertiary Saccharomyces cerevisiae/genetics/growth & dev;"
Notes:"MedlineHuang, Guohong Dougherty, Stephen D Erdman, Scott E eng R03 DE014443/DE/NIDCR NIH HHS/ DE14443-01/DE/NIDCR NIH HHS/ Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't 2009/03/21 Genetics. 2009 May; 182(1):173-89. doi: 10.1534/genetics.108.100073. Epub 2009 Mar 18"

 
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