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Purification of the inducible α‐agglutinin of S. cerevisiae and molecular cloning of the gene
Author(s) -
Hauser Karin,
Tanner Widmar
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81108-1
Subject(s) - microbiology and biotechnology , biochemistry , molecular cloning , molecular mass , agglutinin , peptide sequence , amino acid , gene , glycoprotein , agglutination (biology) , biology , gel electrophoresis , glycosylation , oligonucleotide , chemistry , lectin , genetics , enzyme , antibody
The α‐agglutinin responsible for mating type‐specific agglutination of S. cerevisiae α‐cells has been purified to homogeneity. The glycoprotein released from the cell surface under mild conditions has a relative molecular mass of 200 to 300 kDa as determined by SDS‐gel electrophoresis. The protein moiety corresponds to 68.2 kDa. With an oligonucleotide corresponding to the N‐terminal amino acid sequence, the α‐agglutinin gene has been cloned and sequenced. From the DNA sequence, a protein of 631 amino acids with 12 potential N ‐glycosylation sites is predicted. The carboxy terminal one‐third of the protein is not required for agglutination activity.