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Expanding Role of the Jumonji C Domain as an RNA Hydroxylase |
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| Authors: | Akiko Noma Ryuichiro Ishitani Megumi Kato Asuteka Nagao Osamu Nureki Tsutomu Suzuki |
| Affiliation: | From the ‡Department of Chemistry and Biotechnology, Graduate School of Engineering, University of Tokyo, Hongo, Bunkyo-ku, Tokyo 113-8656 and ;the §Division of Structure Biology, Department of Basic Medical Science, Institute of Medical Science, University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan |
| 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 tRNAPhe by catalyzing hydroxylation. The finding provides an insight into the expanding role of JmjC protein as an RNA hydroxylase. |
| Keywords: | Hydroxylase Mass Spectrometry (MS) Metabolism RNA Modification Transfer RNA (tRNA) JmjC Domain Hydroxywybutosine TYW5 |