Expanding Role of the Jumonji C Domain as an RNA Hydroxylase

• Published in: The Journal of biological chemistry Vol. 285; no. 45; pp. 34503 - 34507
• Main Authors: Noma, Akiko, Ishitani, Ryuichiro, Kato, Megumi, Nagao, Asuteka, Nureki, Osamu, Suzuki, Tsutomu
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 05.11.2010; American Society for Biochemistry and Molecular Biology
• Subjects: Guanine - analogs & derivatives; Guanine - metabolism; HeLa Cells; Humans; Hydroxylase; Hydroxylation; Hydroxywybutosine; JmjC Domain; Mass Spectrometry (MS); Metabolism; Mixed Function Oxygenases - genetics; Mixed Function Oxygenases - metabolism; Protein Structure, Tertiary; RNA; RNA Modification; RNA, Transfer, Phe - genetics; RNA, Transfer, Phe - metabolism; Saccharomyces cerevisiae - genetics; Transfer RNA (tRNA); TYW5; TYW5; Hydroxywybutosine; Hydroxylase; RNA Modification; Mass Spectrometry (MS); Transfer RNA (tRNA); Metabolism; JmjC Domain
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1074/jbc.M110.156398

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.