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Demethylation of H3K27 regulates polycomb recruitment and H2A ubiquitination.

Methylation of histone H3 lysine 27 (H3K27) is a posttranslational modification that is highly correlated with genomic silencing. Here we show that human UTX, a member of the Jumonji C family of proteins, is a di- and trimethyl H3K27 demethylase. UTX occupies the promoters of HOX gene clusters and regulates their transcriptional output by modulating the recruitment of polycomb repressive complex 1 and the monoubiquitination of histone H2A. Moreover, UTX associates with mixed-lineage leukemia (MLL) 2/3 complexes, and during retinoic acid signaling events, the recruitment of the UTX complex to HOX genes results in H3K27 demethylation and a concomitant methylation of H3K4. Our results suggest a concerted mechanism for transcriptional activation in which cycles of H3K4 methylation by MLL2/3 are linked with the demethylation of H3K27 through UTX.

Pubmed ID: 17761849


  • Lee MG
  • Villa R
  • Trojer P
  • Norman J
  • Yan KP
  • Reinberg D
  • Di Croce L
  • Shiekhattar R


Science (New York, N.Y.)

Publication Data

October 19, 2007

Associated Grants

  • Agency: NCI NIH HHS, Id: R01CA090758

Mesh Terms

  • Cell Differentiation
  • Cell Line
  • Cell Line, Tumor
  • DNA-Binding Proteins
  • Embryonic Stem Cells
  • Genes, Homeobox
  • Histone Demethylases
  • Histones
  • Humans
  • Lysine
  • Methylation
  • Multigene Family
  • Neoplasm Proteins
  • Nuclear Proteins
  • Polycomb-Group Proteins
  • Promoter Regions, Genetic
  • Protein Processing, Post-Translational
  • Recombinant Proteins
  • Repressor Proteins
  • Signal Transduction
  • Transcription, Genetic
  • Transcriptional Activation
  • Tretinoin
  • Ubiquitin