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J Biol Chem, Vol. 273, Issue 41, 26298-26304, October 9, 1998
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From the A yeast mutant capable of producing
Man5GlcNAc2 human compatible sugar chains on
glycoproteins was constructed. An expression vector for
Central Laboratories for Key Technology,
KIRIN Brewery Co., Ltd., Yokohama, Kanagawa 236-0004, Japan, the
¶ National Institute of Bioscience and Human Technology, Tsukuba,
Ibaraki 305-0046, Japan, and the Department of Bioengineering,
Faculty of Engineering, Sohka University,
Hachiohji, Tokyo 192-0003, Japan
-1,2-mannosidase with the "HDEL" endoplasmic reticulum retention/retrieval tag was designed and expressed in
Saccharomyces cerevisiae. An in vitro
-1,2-mannosidase assay and Western blot analysis showed that it was
successfully localized in the endoplasmic reticulum. A triple mutant
yeast lacking three glycosyltransferase activities was then transformed
with an -1,2-mannosidase expression vector. The oligosaccharide
structures of carboxypeptidase Y as well as cell surface glycoproteins
were analyzed, and the recombinant yeast was shown to produce a series
of high mannose-type sugar chains including
Man5GlcNAc2. This is the first report of a
recombinant S. cerevisiae able to produce
Man5GlcNAc2-oligosaccharides, the intermediate
for hybrid-type and complex-type sugar chains.
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