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

William G. Kelly, Gerald Warren Hart

Research output: Contribution to journalArticlepeer-review

121 Scopus citations


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 radiolabeling 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 galactosyltrans-ferase-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-GIcNAc). Chromatin is enriched in O-GIcNAc (over 400 pmol/μg of chromatin protein) as compared with total nuclei and other cellular compartments. O-GIcNAc moieties are found on a myriad of chromatin proteins that have diverse types of intermolecular associations with other nuclear components.

Original languageEnglish (US)
Pages (from-to)243-251
Number of pages9
Issue number2
StatePublished - Apr 21 1989

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology


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