Expanding role of the jumonji C domain as an RNA hydroxylase

J Biol Chem. 2010 Nov 5;285(45):34503-7. doi: 10.1074/jbc.M110.156398. Epub 2010 Aug 25.


JmjC (Jumonji C) domain-containing proteins are known to be an extensive family of Fe(II)/2-oxoglutarate-dependent oxygenases involved in epigenetic regulation of gene expression by catalyzing oxidative demethylation of methylated histones. We report here that a human JmjC protein named Tyw5p (TYW5) unexpectedly acts in the biosynthesis of a hypermodified nucleoside, hydroxywybutosine, in tRNA(Phe) by catalyzing hydroxylation. The finding provides an insight into the expanding role of JmjC protein as an RNA hydroxylase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Guanine / analogs & derivatives*
  • Guanine / metabolism
  • HeLa Cells
  • Humans
  • Hydroxylation
  • Mixed Function Oxygenases / genetics
  • Mixed Function Oxygenases / metabolism*
  • Protein Structure, Tertiary
  • RNA, Transfer, Phe / genetics
  • RNA, Transfer, Phe / metabolism*
  • Saccharomyces cerevisiae / genetics


  • RNA, Transfer, Phe
  • hydroxywybutine
  • Guanine
  • Mixed Function Oxygenases