Abstract
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.
MeSH Terms
Amino Acid Sequence
Base Sequence
Cell Wall/enzymology
Cloning, Molecular
DNA, Fungal/genetics,isolation & purification
Escherichia coli/genetics
Genes, Fungal
Glucan 1,3-beta-Glucosidase
Glucosidases/genetics
Molecular Sequence Data
Restriction Mapping
Saccharomyces cerevisiae/enzymology,genetics
Sequence Homology, Nucleic Acid
beta-Glucosidase/genetics
Chemicals
DNA, Fungal
Glucosidases
beta-Glucosidase
Glucan 1,3-beta-Glucosidase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Klebl F
Lehrstuhl für Zellbiologie und Pflanzenphysiologie, Universität Regensburg, Federal Republic of Germany.
Tanner W
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