Glycobiology, Vol 9, 277-283, Copyright © 1999 by Oxford University Press
CW Arendt, W Dawicki and HL Ostergaard
Glucosidase II is a processing enzyme of the endoplasmic reticulum that
functions to hydrolyze two glucose residues in immature N -linked
oligosaccharides attached to newly synthesized polypeptides. We previously
reported the cDNA cloning of the alpha- and beta-subunits of mouse
glucosidase II from T cells following copurification of these proteins with
the highly glycosylated transmembrane protein-tyrosine phosphatase CD45.
Subsequent examination of additional cDNA clones, coupled with partial
genomic DNA sequencing, has revealed that both subunits are encoded by gene
products that undergo alternative splicing in T lymphocytes. The catalytic
alpha-subunit possesses two variably expressed segments, box Alpha1,
consisting of 22 amino acids located proximal to the amino-terminus, and
box Alpha2, composed of 9 amino acids situated between the amino-terminus
and the putative catalytic site in the central region of the molecule. Box
Beta1, a variably expressed 7 amino acid segment in the beta-subunit of
glucosidase II, is located immediately downstream of an acidic stretch near
the carboxyl-terminus. Screening of reverse transcribed RNA by polymerase
chain reaction confirms the variable inclusion of each of these segments in
transcripts obtained from a panel of T-lymphocyte cell lines. Thus,
distinct isoforms of glucosidase II exist that may perform specialized
functions.
ORIGINAL ARTICLES
Alternative splicing of transcripts encoding the alpha- and beta- subunits of mouse glucosidase II in T lymphocytes
Department of Medical Microbiology and Immunology, University of Alberta, Edmonton T6G 2H7, Canada.
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