Validation of the Hsp150 Polypeptide Carrier and HSP150 Promoter in Expression of Rat alpha 2,3-Sialyltransferase in Yeasts

Heterologous glycoproteins usually do not fold properly in yeast cells and fail to leave the endoplasmic reticulum. Here we show that the Hsp150 Delta polypeptide carrier promoted proper folding and secretion of the catalytic ectodomain of rat alpha 2,3-sialyltransferase (ST3Ne) in Pichia pastoris....

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Bibliographic Details
Published in:Biotechnology progress 2003-08, Vol.19 (4), p.1368-1371
Main Authors: Sievi, E, Haenninen, A-L, Salo, H, Kumar, V, Makarow, M
Format: Article
Language:English
Subjects:
a-2,3-sialyltransferase
Hsp150 protein
Pichia pastoris
Saccharomyces cerevisiae
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Summary:Heterologous glycoproteins usually do not fold properly in yeast cells and fail to leave the endoplasmic reticulum. Here we show that the Hsp150 Delta polypeptide carrier promoted proper folding and secretion of the catalytic ectodomain of rat alpha 2,3-sialyltransferase (ST3Ne) in Pichia pastoris. The efficiency of the Hsp150 Delta carrier in P. pastoris and Saccharomyces cerevisiae was at least as high as that of the MF alpha carrier. Most of Hsp150 Delta -ST3Ne and MF alpha -ST3Ne remained noncovalently attached to the cell wall via the ST3Ne portion. The strength of the HSP150 promoter was found to be comparable to that of the GAL1 promoter.
ISSN:8756-7938
DOI:10.1021/bp034035p