RRC ID |
38197
|
Author |
Noma A, Ishitani R, Kato M, Nagao A, Nureki O, Suzuki T.
|
Title |
Expanding role of the jumonji C domain as an RNA hydroxylase.
|
Journal |
J Biol Chem
|
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.
|
Volume |
285(45)
|
Pages |
34503-7
|
Published |
2010-11-5
|
DOI |
10.1074/jbc.M110.156398
|
PII |
S0021-9258(20)46991-1
|
PMID |
20739293
|
PMC |
PMC2966065
|
MeSH |
Guanine / analogs & derivatives*
Guanine / metabolism
HeLa Cells
Humans
Hydroxylation
Mixed Function Oxygenases / genetics
Mixed Function Oxygenases / metabolism*
Protein Structure, Tertiary
RNA, Transfer, Phe / genetics
RNA, Transfer, Phe / metabolism*
Saccharomyces cerevisiae / genetics
|
IF |
4.238
|
Times Cited |
46
|
WOS Category
|
BIOCHEMISTRY & MOLECULAR BIOLOGY
|
Resource |
Human and Animal Cells |
Ehrlich(RCB0142) |