Open AccessMolecular cloning of a cell wall exo-beta-1,3-glucanase from Saccharomyces cerevisiae
Author(s) -
Franz Klebl,
Widmar Tanner
Publication year - 1989
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.171.11.6259-6264.1989
Subject(s) - laminarin , biology , saccharomyces cerevisiae , glucanase , biochemistry , cell wall , yeast , gene , saccharomyces , glucan , peptide sequence , molecular cloning , microbiology and biotechnology , polysaccharide
A major protein of Saccharomyces cerevisiae cell walls is a 29-kilodalton glycoprotein which shows lectinlike binding to beta-1,3-glucan and chitin. It was solubilized by heating isolated cell walls at 90 degrees C and purified to homogeneity by running two high-pressure liquid chromatography columns. With the sequence information of the N terminus and seven peptides, two oligonucleotides were synthesized and the gene was cloned. Its sequence is similar to those of two plant beta-glucanases, and the protein was shown to possess beta-1,3-exoglucanase activity with laminarin as substrate. Haploid yeast cells contained one copy of the gene (BGL2). Gene disruption did not result in a phenotype.