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Heterogeneous glycosylation of the EXG1 gene product accounts for the two extracellular exo‐β‐glucanases of Saccharomyces cerevisiae
Author(s) -
Nebreda A.R.,
Vazquez C.R.,
Villa T.G.,
Villanueva J.R.,
del Rey F.
Publication year - 1987
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(87)80869-4
Subject(s) - saccharomyces cerevisiae , schizosaccharomyces pombe , glycosylation , extracellular , biochemistry , yeast , glycoprotein , gene , biology , endoglycosidase h , cell , golgi apparatus
Two exo‐β‐glucanases of glycoprotein nature can be detected in culture supernatants of Saccharomyces cerevisiae cells. These exo‐β‐glucanases show different M r values and kinetic properties, although they are immunologically related. Their carbohydrate content and the electrophoretic mobility of both endoglycosidase H‐treated exo‐β‐glucanases suggest that they share the same protein fraction. Studies at genetic level relate the production of both extracellular exo‐β‐glucanases with the expression of a single‐copy gene in S. cerevisiae . Expression of this gene in another yeast, Schizosaccharomyces pombe , demonstrates that it codes for a protein with exo‐β‐glucanase activity whose heterogeneous N ‐glycosylation accounts for both extracellular exo‐β‐glucanases of S. cerevisiae .