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. 1989 Apr 21;57(2):243-51.
doi: 10.1016/0092-8674(89)90962-8.

Glycosylation of chromosomal proteins: localization of O-linked N-acetylglucosamine in Drosophila chromatin

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Glycosylation of chromosomal proteins: localization of O-linked N-acetylglucosamine in Drosophila chromatin

W G Kelly et al. Cell. .

Erratum in

  • Cell 1989 Jul 28;58(2):following 419

Abstract

Drosophila polytene chromosomes contain a surprisingly large amount of terminal N-acetylglucosamine (GlcNAc) residues along their lengths, as determined by staining with a fluorescently tagged lectin, wheat germ agglutinin (FITC-WGA) and by specific radio-labeling with bovine galactosyltransferase and UDP-[3H]galactose. FITC-WGA intensely stains polytene chromosomes in a distinctive banding pattern in which condensed chromatin is brightly labeled and transcriptionally active "puff" regions are less intensely stained. Biochemical analyses of galactosyltransferase-radiolabeled chromatin indicates that nearly all of the chromatin-associated GlcNAc moieties exist as single monosaccharide residues attached to protein by an O-linkage (O-GlcNAc). Chromatin is enriched in O-GlcNAc (over 400 pmol/micrograms of chromatin protein) as compared with total nuclei and other cellular compartments. O-GlcNAc moieties are found on a myriad of chromatin proteins that have diverse types of intermolecular associations with other nuclear components.

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