Reference: Holkeri H, et al. (1996) Glycosylation of rat NGF receptor ectodomain in the yeast Saccharomyces cerevisiae. FEBS Lett 383(3):255-8

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Abstract


Here we studied the glycosylation of a mammalian protein, the ectodomain of rat nerve growth factor receptor (NGFRe), in Saccharomyces cerevisiae. NGFRe is secreted to the culture medium of S. cerevisiae if it is fused to a polypeptide (hsp 150 delta) carrier. The hsp 150 delta-carrier has 95 serine and threonine residues, which were extensively O-glycosylated. In spite of 41 potential sites, NGFRe lacked O-glycans, whether fused to the carrier or not. Distortion of the conformation of NGFRe by inhibition of disulfide formation did not promote O-glycosylation, whereas N-glycosylation was enhanced. Thus, the serine and threonine residues of the hsp 150 delta-NGFRe fusion protein were highly selectively O-glycosylated.

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Journal Article | Research Support, Non-U.S. Gov't
Authors
Holkeri H, Simonen M, Pummi T, Vihinen H, Makarow M
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