Identification of JmjC domain-containing UTX and JMJD3 as histone H3 lysine 27 demethylases

Covalent modifications of histones, such as acetylation and methylation, play important roles in the regulation of gene expression. Histone lysine methylation has been implicated in both gene activation and repression, depending on the specific lysine (K) residue that becomes methylated and the state of methylation (mono-, di-, or trimethylation). Methylation on K4, K9, and K36 of histone H3 has been shown to be reversible and can be removed by site-specific demethylases. However, the enzymes that antagonize methylation on K27 of histone H3 (H3K27), an epigenetic mark important for embryonic stem cell maintenance, Polycomb-mediated gene silencing, and X chromosome inactivation have been elusive. Here we show…

• NI
  National Institutes of Health

  Award: N01-CO-12400
• NC
  National Cancer Institute

  Award: N01-CO-12400
• NI
  National Institute of Diabetes and Digestive and Kidney Diseases