Bedoukian   RussellIPM   RussellIPM   Piezoelectric Micro-Sprayer


Home
Animal Taxa
Plant Taxa
Semiochemicals
Floral Compounds
Semiochemical Detail
Semiochemicals & Taxa
Synthesis
Control
Invasive spp.
References

Abstract

Guide

Alphascents
Pherobio
InsectScience
E-Econex
Counterpart-Semiochemicals
Print
Email to a Friend
Kindly Donate for The Pherobase

« Previous Abstract"The evolutionary trajectories of the individual amygdala nuclei in the common shrew, guinea pig, rabbit, fox and pig: A consequence of embryological fate and mosaic-like evolution"    Next AbstractA distributed parameter physiologically-based pharmacokinetic model for dermal and inhalation exposure to volatile organic compounds »

Mol Cell Biol


Title:The AGA1 product is involved in cell surface attachment of the Saccharomyces cerevisiae cell adhesion glycoprotein a-agglutinin
Author(s):Roy A; Lu CF; Marykwas DL; Lipke PN; Kurjan J;
Address:"Department of Biological Sciences, Columbia University, New York, New York 10027"
Journal Title:Mol Cell Biol
Year:1991
Volume:11
Issue:8
Page Number:4196 - 4206
DOI: 10.1128/mcb.11.8.4196-4206.1991
ISSN/ISBN:0270-7306 (Print) 1098-5549 (Electronic) 0270-7306 (Linking)
Abstract:"Saccharomyces cerevisiae a and alpha cells express the complementary cell surface glycoproteins a-agglutinin and alpha-agglutinin, respectively, which interact with one another to promote cellular aggregation during mating. Treatment of S. cerevisiae a cells with reducing agents releases the binding subunit of a-agglutinin, which has been purified and characterized; little biochemical information on the overall structure of a-agglutinin is available. To characterise a-agglutinin structure and function, we have used a genetic approach to clone an a-agglutinin structural gene (AGAI). Mutants with a-specific agglutination defects were isolated, the majority of which fell into a single complementation group, called aga1. The aga1 mutants showed wild-type pheromone production and response, efficient mating on solid medium, and a mating defect in liquid medium; these phenotypes are characteristic of agglutinin mutants. The AGA1 gene was cloned by complementation; the gene sequence indicated that it could encode a protein of 725 amino acids with high serine and threonine content, a putative N-terminal signal sequence, and a C-terminal hydrophobic sequence similar to signals for the attachment to glycosyl phosphatidylinositol anchors. Active a-agglutinin binding subunit is secreted by aga1 mutants, indicating that AGA1 is involved in cells surface attachment of a-agglutinin. This result suggests that AGA1 encodes a protein with functional similarity to the core subunits of a-agglutinin analogs from other budding yeasts. Unexpectedly, the AGA1 transcript was expressed and induced by pheromone in both a and alpha cells, suggesting that the a-specific expression of active a-agglutinin results only from a-specific regulation of the a-agglutinin binding subunit"
Keywords:"Agglutination Amino Acid Sequence Base Sequence Cell Adhesion Molecules Cell Membrane/physiology Crosses, Genetic DNA, Fungal/genetics/isolation & purification Escherichia coli/genetics Fungal Proteins/*genetics Genes, Dominant *Genes, Fungal Genetic Comp;"
Notes:"MedlineRoy, A Lu, C F Marykwas, D L Lipke, P N 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. 1991/08/01 Mol Cell Biol. 1991 Aug; 11(8):4196-206. doi: 10.1128/mcb.11.8.4196-4206.1991"

 
Back to top
 
Citation: El-Sayed AM 2024. The Pherobase: Database of Pheromones and Semiochemicals. <http://www.pherobase.com>.
© 2003-2024 The Pherobase - Extensive Database of Pheromones and Semiochemicals. Ashraf M. El-Sayed.
Page created on 27-12-2024