作为 RNA 羟化酶， jumonji C 结构域的作用不断扩大。
Expanding role of the jumonji C domain as an RNA hydroxylase.
机构信息
Department of Chemistry and Biotechnology, Graduate School of Engineering, University of Tokyo, Hongo, Bunkyo-ku, Tokyo 113-8656, Japan.
出版信息
J Biol Chem. 2010 Nov 5;285(45):34503-7. doi: 10.1074/jbc.M110.156398. Epub 2010 Aug 25.
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.
摘要
JmjC（Jumonji C）结构域蛋白是一类广泛存在的 Fe(II)/2- 氧戊二酸依赖的氧合酶家族，通过催化组蛋白的氧化脱甲基化，参与基因表达的表观遗传调控。我们在此报告，一种名为 Tyw5p（TYW5）的人源 JmjC 蛋白通过催化羟化作用，出乎意料地在 tRNA(Phe)中参与羟化修饰核苷羟基wybutosine 的生物合成。这一发现为 JmjC 蛋白作为 RNA 羟化酶的作用不断扩大提供了新的认识。
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