Expanding Role of the Jumonji C Domain as an RNA Hydroxylase

被引：57
作者：
Noma, Akiko
Ishitani, Ryuichiro [2 ]
Kato, Megumi [2 ]
Nagao, Asuteka
Nureki, Osamu [2 ]
Suzuki, Tsutomu [1 ]
机构：
[1] Univ Tokyo, Grad Sch Engn, Dept Chem & Biotechnol, Bunkyo Ku, Tokyo 1138656, Japan
[2] Univ Tokyo, Inst Med Sci, Dept Basic Med Sci, Div Struct Biol,Minato Ku, Tokyo 1088639, Japan
来源：
JOURNAL OF BIOLOGICAL CHEMISTRY | 2010年 / 285卷 / 45期
基金：
日本学术振兴会;
关键词：
TRANSFER-RIBONUCLEIC-ACID; Y BASE; WYBUTOSINE; NUCLEOSIDE; IDENTIFICATION; ENZYME; PHE;
D O I：
10.1074/jbc.M110.156398
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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.
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收藏
页码：34503 / 34507
页数：5
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