Dynamic glycosylation of nuclear and cytosolic proteins: Cloning and characterization of a unique O-GlcNAc transferase with multiple tetratricopeptide repeats

Lisa K. Kreppel, Melissa A. Blomberg, Gerald Warren Hart

Research output: Contribution to journalArticle

Abstract

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.

Original languageEnglish (US)
Pages (from-to)9308-9315
Number of pages8
JournalJournal of Biological Chemistry
Volume272
Issue number14
DOIs
StatePublished - Apr 4 1997
Externally publishedYes

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Glycosylation
Cloning
Nuclear Proteins
Organism Cloning
Proteins
Glycosyltransferases
Phosphorylation
Genes
Signal transduction
Tandem Repeat Sequences
Acetylglucosamine
Sequence Homology
O-GlcNAc transferase
Eukaryota
Cytosol
Protein-Tyrosine Kinases
Tyrosine
Signal Transduction
Catalytic Domain
Enzymes

ASJC Scopus subject areas

  • Biochemistry

Cite this

Dynamic glycosylation of nuclear and cytosolic proteins : Cloning and characterization of a unique O-GlcNAc transferase with multiple tetratricopeptide repeats. / Kreppel, Lisa K.; Blomberg, Melissa A.; Hart, Gerald Warren.

In: Journal of Biological Chemistry, Vol. 272, No. 14, 04.04.1997, p. 9308-9315.

Research output: Contribution to journalArticle

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