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

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


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Acetylglucosamine / analysis*
  • Acetylglucosamine / metabolism
  • Animals
  • Chromatin / analysis*
  • Chromatin / metabolism
  • Chromosome Banding
  • Drosophila melanogaster
  • Galactose / metabolism
  • Galactosyltransferases
  • Glucosamine / analogs & derivatives*
  • Glycoproteins / analysis
  • Glycoproteins / metabolism
  • Glycosylation


  • Chromatin
  • Glycoproteins
  • Galactosyltransferases
  • Glucosamine
  • Acetylglucosamine
  • Galactose