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PMID: 1756718 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Saccharomyces cerevisiae a- and alpha-agglutinin: characterization of their molecular interaction.

The EMBO journal ·Vol. 10 ·No. 13 ·1991-12-00 ·Pages 4081-8

Cappellaro C, Hauser K, Mrśa V, Watzele M, Watzele G, Gruber C, Tanner W

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.

MeSH Terms
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,metabolism Pheromones/metabolism Polymerase Chain Reaction RNA, Fungal/analysis Saccharomyces cerevisiae/metabolism Saccharomyces cerevisiae Proteins Trypsin
Chemicals
Fungal Proteins Peptides Pheromones RNA, Fungal Saccharomyces cerevisiae Proteins a-agglutinin protein, S cerevisiae Mating Factor Trypsin Diethyl Pyrocarbonate
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Cappellaro C
Lehrstuhl für Zellbiologie und Pflanzenphysiologie, Universität Regensburg, FRG.
Hauser K
Mrśa V
Watzele M
Watzele G
Gruber C
Tanner W
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1991-12-00
Pages
4081-8
Language
English
Region
England
NLM ID
8208664
PMCID
PMC453156
Subset
IM
Databases
GENBANK
M62511, M62512, M62513, M62514, M62515, S65080, S65083, S72668, X62877, X62936
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