Role of glycosylation in secretion of yeast acid phosphatase

FEBS Letters

Ries, Blanka¹  Mrša, Vladimir¹  Mildner, Pavao¹  Barbarić, Slobodan¹ 

[1] Laboratory of Biochemistry, Faculty of Food Technology and Biotechnology, Pierottijeva 6, 41000 Zagreb, Yugoslavia

关键词: Glycosylation;    Protein secretion;    Acid phosphatase;    (Saccharomyces cerevisiae);    APase;    acid phosphatase;    TM;    tunicamycin;    ER;    endoplasmic reticulum;   

DOI  :  10.1016/0014-5793(87)80658-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The minimal glycosylation requirement for acid phosphatase secretion and activity was investigated using tunicamycin, an inhibitor of protein glycosylation, and a yeast mutant defective in the synthesis of oligosaccharide outer chains. The results obtained show that outer chain addition is not essential for secretion of active enzyme and that only 4 core chains, out of 8 normally attached to a protein subunit, are sufficient for enzyme transport to the periplasmic space. Enzyme forms with less than 4 chains were retained in membranes of endoplasmic reticulum. Secreted underglycosylated enzyme forms are partially or completely inactive.

【 授权许可】

Unknown