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.
Akiko Noma  1 ,  Ryuichiro Ishitani ,  Megumi Kato ,  Asuteka Nagao ,  Osamu Nureki ,  Tsutomu Suzuki
Affiliations
  • 1. Department of Chemistry and Biotechnology, Graduate School of Engineering, University of Tokyo, Hongo, Bunkyo-ku, Tokyo 113-8656, Japan.
PMID: 20739293 DOI: 10.1074/jbc.M110.156398
Abstract

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.