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Saccharomyces cerevisiae a‐ and alpha‐agglutinin: characterization of their molecular interaction.
Author(s) -
Cappellaro C.,
Hauser K.,
Mrśa V.,
Watzele M.,
Watzele G.,
Gruber C.,
Tanner W.
Publication year - 1991
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1991.tb04984.x
Subject(s) - biology , saccharomyces cerevisiae , alpha (finance) , agglutinin , genetics , computational biology , biochemistry , yeast , lectin , medicine , construct validity , nursing , patient satisfaction
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.