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J. Biol. Chem., Vol. 262, Issue 31, 14847-14850, 11, 1987
GD Holt, RS Haltiwanger, CR Torres and GW Hart
Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.
Previously we reported that the novel protein-saccharide linkage, O- linked N-acetylglucosamine (GlcNAc), is found in abundance on proteins associated with the cytoplasmic and nucleoplasmic faces of the nuclear pore complex. Here we demonstrate that O-GlcNAc moieties are also added to human erythrocyte cytoplasmic proteins. Intact or permeabilized erythrocytes, as well as subcellular fractions, were labeled with bovine milk galactosyltransferase and UDP-[3H] galactose. The proportion of the incorporated label found on O-GlcNAc was determined by a variety of chemical and enzymatic techniques. The bulk of the O- GlcNAc residues are found in the cytoplasm of erythrocytes, the majority of which are on an as yet unidentified 65-kDa protein. In addition, we have determined that Band 4.1, a protein which serves as a bridge joining the cytoskeleton to the inner surface of the plasma membrane in erythrocytes, also contains O-GlcNAc moieties. One of the sites of O-GlcNAc addition has been localized to the last 117 amino acids of the carboxy terminus of Band 4.1.
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