Drosophila UTX is a histone H3 Lys27 demethylase that colocalizes with the elongating form of RNA polymerase II

Edwin R. Smith, Gyu Lee Min, Benjamin Winter, Nathan M. Droz, Joel C. Eissenberg, Ramin Shiekhattar, Ali Shilatifard

Research output: Contribution to journalArticle

95 Citations (Scopus)

Abstract

Histone H3 methylation at Lys27 (H3K27 methylation) is a hallmark of silent chromatin, while H3K4 methylation is associated with active chromatin regions. Here we report that a Drosophila JmjC family member, dUTX, specifically demethylates di- and trimethylated but not monomethylated H3K27. dUTX localization on chromatin correlates with the elongating form of RNA polymerase II (Pol II), and dUTX can associate with Pol II. Furthermore, heat shock induction results in the recruitment of dUTX to the hsp70 gene, like that of several other Pol II elongation factors. Our data indicate that dUTX is intimately associated with actively transcribed genes and may provide a paradigm for how H3K27 demethylation is required for the activation of preinitiated Pol II on transcriptionally poised genes.

Original languageEnglish (US)
Pages (from-to)1041-1046
Number of pages6
JournalMolecular and Cellular Biology
Volume28
Issue number3
DOIs
StatePublished - Feb 2008
Externally publishedYes

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RNA Polymerase II
Histones
Methylation
Drosophila
Chromatin
Genes
Peptide Elongation Factors
Shock
Hot Temperature

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this

Drosophila UTX is a histone H3 Lys27 demethylase that colocalizes with the elongating form of RNA polymerase II. / Smith, Edwin R.; Min, Gyu Lee; Winter, Benjamin; Droz, Nathan M.; Eissenberg, Joel C.; Shiekhattar, Ramin; Shilatifard, Ali.

In: Molecular and Cellular Biology, Vol. 28, No. 3, 02.2008, p. 1041-1046.

Research output: Contribution to journalArticle

Smith, Edwin R. ; Min, Gyu Lee ; Winter, Benjamin ; Droz, Nathan M. ; Eissenberg, Joel C. ; Shiekhattar, Ramin ; Shilatifard, Ali. / Drosophila UTX is a histone H3 Lys27 demethylase that colocalizes with the elongating form of RNA polymerase II. In: Molecular and Cellular Biology. 2008 ; Vol. 28, No. 3. pp. 1041-1046.
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