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(Received for publication, November 26, 1996, and in revised form, January 25, 1997)
,
From the Department of Biochemistry and Molecular Genetics Schools
of Medicine/Dentistry, University of Alabama at Birmingham Station,
Birmingham, Alabama 35294 and the O-Linked
N-acetylglucosamine (O-GlcNAc) glycosylation is
a dynamic modification of eukaryotic nuclear and cytosolic proteins analogous to protein phosphorylation. We have cloned and characterized a novel gene for an O-GlcNAc transferase (OGT) that shares
no sequence homology or structural similarities with other
glycosyltransferases. The OGT gene is highly conserved (up to 80%
identity) in all eukaryotes examined. Unlike previously described
glycosyltransferases, OGT is localized to the cytosol and nucleus. The
OGT protein contains multiple tandem repeats of the tetratricopeptide
repeat motif. The presence of tetratricopeptide repeats, which can
mediate protein-protein interactions, suggests that OGT may be
regulated by protein interactions that are independent of the enzyme's
catalytic site. The OGT is also modified by tyrosine phosphorylation,
indicating that tyrosine kinase signal transduction cascades may play a
role in modulating OGT activity.
Department of
Biological Chemistry, The Johns Hopkins University School of
Medicine, Baltimore, Maryland 21205
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