Glycosylation of rat NGF receptor ectodomain in the yeast Saccharomyces cerevisiae

FEBS Letters

Pummi, Tiina¹  Vihinen, Helena¹  Makarow, Marja¹  Simonen, Marjo¹  Holkeri, Heidi¹ 

[1] Institute of Biotechnology, Biocentre 1A, P.O. Box 56 (Viikinkaari 9), 00014 University of Helsinki, Helsinki, Finland

关键词: Glycosylation;    Yeast;    Secretion;    NGF receptor;    Protein folding;   

DOI  :  10.1016/0014-5793(96)00264-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Here we studied the glycosylation of a mammalian protein, the ectodomain of rat nerve growth factor receptor (NGFR _e ), in Saccharomyces cerevisiae. NGFR _e is secreted to the culture medium of S. cerevisiae if it is fused to a polypeptide (hsp150Δ) carrier. The hsp150Δ-carrier has 95 serine and threonine residues, which were extensively O-glycosylated. In spite of 41 potential sites, NGF _e lacked O-glycans, whether fused to the carrier or not. Distortion of the conformation of NGFR _e by inhibition of disulfide formation did not promote O-glycosylation, whereas N-glycosylation was enhanced. Thus, the serine and threonine residues of the hsp150Δ-NGFR _e fusion protein were highly selectively O-glycosylated.

【 授权许可】

Unknown