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J. Biol. Chem., Vol. 269, Issue 30, 19321-19330, Jul, 1994
DL Dong and GW Hart
Glycosylation of nuclear and cytoplasmic proteins by O-linked N-
acetylglucosamine (O-GlcNAc) monosaccharides is an abundant, ubiquitous,
and transient post-translational modification. To characterize enzymes
involved in removal of these sugars, a neutral and cytoplasmic
N-acetyl-beta-D-glucosaminidase (O-GlcNAcase) with strong selectivity for
O-GlcNAc-synthetic glycopeptides has been purified over 22,000-fold from
rat spleen homogenate. The purified O-GlcNAcase has two major polypeptides
of apparent M(r) = 54,000 (alpha subunit) and M(r) = 51,000 (beta subunit).
Enzyme activity sediments at M(r) = 106,000 on sucrose gradients,
indicating that the native O-GlcNAcase is an alpha beta heterodimer. The
O-GlcNAcase also shows substantially stronger relative activity against
O-GlcNAc-synthetic glycopeptides than other hexosaminidases. Unlike acidic
lysosomal hexosaminidases, O- GlcNAcase is not inhibited by GalNAc or its
analogs, has no other detectable glycosidase activities, and does not
cross-react with antibodies against acidic hexosaminidases. Subcellular
fractionation and latency studies demonstrate the cytoplasmic and
nucleoplasmic localization of the enzyme and its ubiquitous presence in
tissues. These studies suggest that O-GlcNAcase is involved in the
regulated removal of O-GlcNAc from O-GlcNAc-bearing glycoproteins in the
nucleoplasmic and cytoplasmic compartments of cells.
Purification and characterization of an O-GlcNAc selective N-acetyl- beta-D-glucosaminidase from rat spleen cytosol
Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.
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Y. Gao, L. Wells, F. I. Comer, G. J. Parker, and G. W. Hart Dynamic O-Glycosylation of Nuclear and Cytosolic Proteins. CLONING AND CHARACTERIZATION OF A NEUTRAL, CYTOSOLIC beta -N-ACETYLGLUCOSAMINIDASE FROM HUMAN BRAIN J. Biol. Chem., March 23, 2001; 276(13): 9838 - 9845. [Abstract] [Full Text] [PDF]
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L. Wells, Y. Gao, J. A. Mahoney, K. Vosseller, C. Chen, A. Rosen, and G. W. Hart Dynamic O-Glycosylation of Nuclear and Cytosolic Proteins. FURTHER CHARACTERIZATION OF THE NUCLEOCYTOPLASMIC beta -N-ACETYLGLUCOSAMINIDASE, O-GlcNAcase J. Biol. Chem., January 11, 2002; 277(3): 1755 - 1761. [Abstract] [Full Text] [PDF]
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F. I. Comer and G. W. Hart O-Glycosylation of Nuclear and Cytosolic Proteins. DYNAMIC INTERPLAY BETWEEN O-GlcNAc AND O-PHOSPHATE J. Biol. Chem., September 15, 2000; 275(38): 29179 - 29182. [Full Text] [PDF]
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R. Shafi, S. P. N. Iyer, L. G. Ellies, N. O'Donnell, K. W. Marek, D. Chui, G. W. Hart, and J. D. Marth The O-GlcNAc transferase gene resides on the X chromosome and is essential for embryonic stem cell viability and mouse ontogeny PNAS, May 23, 2000; 97(11): 5735 - 5739. [Abstract] [Full Text] [PDF]
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X. Yang, K. Su, M. D. Roos, Q. Chang, A. J. Paterson, and J. E. Kudlow O-linkage of N-acetylglucosamine to Sp1 activation domain inhibits its transcriptional capability PNAS, June 5, 2001; 98(12): 6611 - 6616. [Abstract] [Full Text] [PDF]
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