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(Received for publication, June 17, 1996, and in revised form, August 20, 1996)
From the Department of Cell Biology, Yale University School of
Medicine, P.O. Box 208002, New Haven, Connecticut 06520-8002
Trimming of glucoses from N-linked
core glycans on newly synthesized glycoproteins occurs sequentially
through the action of glucosidases I and II in the endoplasmic
reticulum (ER). We isolated enzymatically active glucosidase II from
rat liver and found that, in contrast with previous reports, it
contains two subunits (
Volume 271, Number 44,
Issue of November 1, 1996
pp. 27509-27516
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
and 
). Sequence analysis of peptides
derived from them allowed us to identify their corresponding human
cDNA sequences. The sequence of the subunit predicted a soluble
protein (104 kDa) devoid of known signals for residence in the ER. It
showed homology with several other glucosidases but not with
glucosidase I. Among the homologues, we identified a
Saccharomyces cerevisiae gene, which we showed by gene
disruption experiments to be the functional catalytic subunit of
glucosidase II. The disrupted yeast strains had no detectable growth
defect. The sequence of the subunit (58 kDa) showed no sequence
homology with other known proteins. It encoded a soluble protein rich
in glutamic and aspartic acid with a putative ER retention signal
(HDEL) at the C terminus. This suggested that the subunit is
responsible for the ER localization of the enzyme.
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