High impact information on AGA2

• 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 [1].
• Mutagenesis of AGA2 identified only C-terminal residues of Aga2p as being essential for binding activity [2].
• Cell wall attachment of Aga2p is mediated through two disulfide bonds to Aga1p (Cappellaro, C., Baldermann, C., Rachel, R., and Tanner, W. (1994) EMBO J. 13, 4737-4744) [2].
• Mutation of either or both Aga2p cysteine residues eliminated stabilization of Aga2p [2].
• a-Agglutinin from Saccharomyces cerevisiae is a cell adhesion glycoprotein expressed on the surface of cells of a mating type and consists of an anchorage subunit Aga1p and a receptor binding subunit Aga2p [2].

Biological context of AGA2

• AGA2 was mapped to the left arm of chromosome VII approximately 28 cM from the centromere [3].
• The Saccharomyces cerevisiae cell adhesion protein a-agglutinin is composed of an anchorage subunit (Aga1p) and an adhesion subunit (Aga2p) [3].

Associations of AGA2 with chemical compounds

• Thus the roles of Aga1p include both cell wall anchorage and cysteine-dependent conformational restriction of the binding subunit Aga2p [2].
• A 30-residue Cys-rich Aga1p fragment was partially active in stabilization of Aga2p activity [2].
• Under the treatment by the SH-compound (dithiothreitol), in which Agalpha2p is easily released into the medium from the intact cell surface, the Aga1p and Aga2p fusion protein was a good tool to make clear the role of the disulphide linkages [4].
• These results proved that the constructed Aga1p-Aga2p fusion protein was enoughly functional for the interaction with the Agalpha1 protein, and that this phenomenon occurred dependent on glucose concentration, but independent of the peptide pheromones secreted by the cells of the opposite mating types [4].
• Consequently we rebuilt pYD1 tethering the scFv off the NH(2) terminus of Aga2 [5].

Other interactions of AGA2

• Most of the a-specific agglutination-defective mutants isolated previously were defective in AGA1; a single mutant (La199) was a candidate for an aga2 mutant [3].

Analytical, diagnostic and therapeutic context of AGA2

• Circular dichroism of the complex revealed a mixed alpha/beta structure, whereas Aga2p alone had no periodic secondary structure [2].

References