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

William G. Kelly; Gerald Warren Hart

doi:10.1016/0092-8674(89)90962-8

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

William G. Kelly, Gerald Warren Hart

School of Medicine

Research output: Contribution to journal › Article › peer-review

121 Scopus citations

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 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 language	English (US)
Pages (from-to)	243-251
Number of pages	9
Journal	Cell
Volume	57
Issue number	2
DOIs	https://doi.org/10.1016/0092-8674(89)90962-8
State	Published - Apr 21 1989

ASJC Scopus subject areas

Cell Biology
Molecular Biology

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title = "Glycosylation of chromosomal proteins: Localization of O-linked N-acetylglucosamine in Drosophila chromatin",

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 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.",

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T2 - Localization of O-linked N-acetylglucosamine in Drosophila chromatin

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AU - Hart, Gerald Warren

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N2 - 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.

AB - 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.

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

Abstract

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