| Literature DB >> 20739293 |
Akiko Noma1, Ryuichiro Ishitani, Megumi Kato, Asuteka Nagao, Osamu Nureki, Tsutomu Suzuki.
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.Entities:
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Year: 2010 PMID: 20739293 PMCID: PMC2966065 DOI: 10.1074/jbc.M110.156398
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157