Heterogeneous glycosylation of the EXG1 gene product accounts for the two extracellular exo‐β‐glucanases of Saccharomyces cerevisiae

FEBS Letters

Villanueva, J.R.¹  Nebreda, A.R.¹  del Rey, F.¹  Vazquez, C.R.¹  Villa, T.G.¹ 

[1] Instituto de Microbiologia Bioquimica, CSIC and Departamento de Microbiologia, Facultad de Biologia, Universidad de Salamanca, 37071 Salamanca, Spain

关键词: β-Glucanase;    Extracellular enzyme;    Glycosylation;    Cell wall;    (Yeast);    endo H;    endo-β-N-acetylglucosaminidase H;    MUG;    4-methylumbelliferyl-β-D-glucoside;    PAGE;    polyacrylamide gel electrophoresis;   

DOI  :  10.1016/0014-5793(87)80869-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown