| Title: | Saccharomyces cerevisiae a- and alpha-agglutinin: characterization of their molecular interaction |
| Author(s): | Cappellaro C; Hauser K; Mrsa V; Watzele M; Watzele G; Gruber C; Tanner W; |
| Address: | "Lehrstuhl fur Zellbiologie und Pflanzenphysiologie, Universitat Regensburg, FRG" |
| DOI: | 10.1002/j.1460-2075.1991.tb04984.x |
| ISSN/ISBN: | 0261-4189 (Print) 1460-2075 (Electronic) 0261-4189 (Linking) |
| Abstract: | "An O-glycosylated protein of approximately 18 kDa responsible for mating type specific agglutination has been isolated from Saccharomyces cerevisiae a cells, purified to homogeneity and via peptide sequences the gene was cloned by PCR. An open reading frame codes for a protein of 69 amino acids. A minimum of five serine and five threonine residues of the mature protein are glycosylated. alpha-Agglutinin is a highly N-glycosylated protein of approximately 250 kDa. Both purified agglutinins form a specific 1:1 complex in vitro. Pretreatment of alpha-agglutinin, but not of alpha-agglutinin, with diethylpyrocarbonate (DEPC) prevents formation of the complex; treatment of alpha-agglutinin in the presence of alpha-agglutinin protects the former from DEPC inactivation. By carboxy terminal shortening of the alpha-agglutinin gene and by replacing three of its eight histidyl residues by arginine, the active region of alpha-agglutinin for interaction with alpha-agglutinin has been defined. Neither the N- nor the O-linked saccharides of the two agglutinins seem to be essential for their interaction" |
| Keywords: | "Base Sequence Blotting, Northern Cloning, Molecular Diethyl Pyrocarbonate/chemistry Fungal Proteins/genetics/*metabolism Glycosylation Mating Factor Molecular Sequence Data Mutagenesis, Site-Directed Open Reading Frames Peptide Mapping Peptides/genetics/*;" |
| Notes: | "MedlineCappellaro, C Hauser, K Mrsa, V Watzele, M Watzele, G Gruber, C Tanner, W eng Research Support, Non-U.S. Gov't England 1991/12/01 EMBO J. 1991 Dec; 10(13):4081-8. doi: 10.1002/j.1460-2075.1991.tb04984.x" |
