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Drosophila O-GlcNAc transferase (OGT) is encoded by the Polycomb group (PcG) gene, super sex combs (sxc)

Academic Article
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Overview

authors

  • Sinclair, D. A. R.
  • Syrzycka, M.
  • Macauley, Matthew
  • Rastgardani, T.
  • Komljenovic, I.
  • Vocadlo, D. J.
  • Brock, H. W.
  • Honda, B. M.

publication date

  • August 2009

journal

  • Proceedings of the National Academy of Sciences of the United States of America  Journal

abstract

  • O-linked N-acetylglucosamine transferase (OGT) reversibly modifies serine and threonine residues of many intracellular proteins with a single beta-O-linked N-acetylglucosamine residue (O-GlcNAc), and has been implicated in insulin signaling, neurodegenerative disease, cellular stress response, and other important processes in mammals. OGT also glycosylates RNA polymerase II and various transcription factors, which suggests that it might be directly involved in transcriptional regulation. We report here that the Drosophila OGT is encoded by the Polycomb group (PcG) gene, super sex combs (sxc). Furthermore, major sites of O-GlcNAc modification on polytene chromosomes correspond to PcG protein binding sites. Our results thus suggest a direct role for O-linked glycosylation by OGT in PcG-mediated epigenetic gene silencing, which is important in developmental regulation, stem cell maintenance, genomic imprinting, and cancer. In addition, we observe rescue of sxc lethality by a human Ogt cDNA transgene; thus Drosophila may provide an ideal model to study important functional roles of OGT in mammals.

subject areas

  • Animals
  • Binding Sites
  • Chromatin Immunoprecipitation
  • Chromosome Mapping
  • Chromosomes
  • Drosophila Proteins
  • Drosophila melanogaster
  • Genes, Insect
  • Humans
  • Mutation
  • N-Acetylglucosaminyltransferases
  • Polycomb-Group Proteins
  • Protein Binding
  • Protein Processing, Post-Translational
  • Protein Transport
  • Repressor Proteins
  • Transgenes
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Research

keywords

  • O-glycosylation
  • epigenetic
  • gene silencing
  • glycosyl transferase
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Identity

PubMed Central ID

  • PMC2726349

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.0904638106

PubMed ID

  • 19666537
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Additional Document Info

start page

  • 13427

end page

  • 13432

volume

  • 106

issue

  • 32

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