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Glycosylation of rat NGF receptor ectodomain in the yeast Saccharomyces cerevisiae
Author(s) -
Holkeri Heidi,
Simonen Marjo,
Pummi Tiina,
Vihinen Helena,
Makarow Marja
Publication year - 1996
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(96)00264-5
Subject(s) - ectodomain , glycosylation , saccharomyces cerevisiae , biochemistry , threonine , chemistry , serine , yeast , receptor , phosphorylation
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 hsp150 Δ ‐NGFR e fusion protein were highly selectively O ‐glycosylated.