| Autor: |
Cappellaro, C., Hauser, K., Mrśa, V., Watzele, M., Watzele, G., Gruber, C., Tanner, W. |
| Zdroj: |
The EMBO Journal; December 1991, Vol. 10 Issue: 13 p4081-4088, 8p |
| Abstrakt: |
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. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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