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Recruitment of O-GlcNAc transferase to promoters by corepressor mSin3A: coupling protein O-GlcNAcylation to transcriptional repression.

Transcription factors and RNA polymerase II can be modified by O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides at serine or threonine residues, yet the precise functional roles of this modification are largely unknown. Here, we show that O-GlcNAc transferase (OGT), the enzyme that catalyzes this posttranslational modification, interacts with a histone deacetylase complex by binding to the corepressor mSin3A. Functionally, OGT and mSin3A cooperatively repress transcription in parallel with histone deacetylation. We propose that mSin3A targets OGT to promoters to inactivate transcription factors and RNA polymerase II by O-GlcNAc modification, which acts in concert with histone deacetylation to promote gene silencing in an efficient and specific manner.

Pubmed ID: 12150998

Authors

  • Yang X
  • Zhang F
  • Kudlow JE

Journal

Cell

Publication Data

July 12, 2002

Associated Grants

None

Mesh Terms

  • Animal Population Groups
  • Animals
  • COS Cells
  • Gene Expression Regulation
  • Gene Silencing
  • Genes, Reporter
  • Glycoproteins
  • Histone Deacetylases
  • Humans
  • N-Acetylglucosaminyltransferases
  • Promoter Regions, Genetic
  • Repressor Proteins
  • Transcription Factors
  • Transcription, Genetic
  • Tumor Cells, Cultured