Expanding role of the jumonji C domain as an RNA hydroxylase.
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.
Noma
Akiko
A
Department of Chemistry and Biotechnology, Graduate School of Engineering, University of Tokyo, Hongo, Bunkyo-ku, Tokyo 113-8656, Japan.
Ishitani
Ryuichiro
R
Kato
Megumi
M
Nagao
Asuteka
A
Nureki
Osamu
O
Suzuki
Tsutomu
T
D006147:Guanine / Q000031:analogs & derivatives* / Q000378:metabolism; D006367:HeLa Cells; D006801:Humans; D006900:Hydroxylation; D006899:Mixed Function Oxygenases / Q000235:genetics / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D012360:RNA, Transfer, Phe / Q000235:genetics / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000235:genetics
D012360:RNA, Transfer, Phe; C114501:hydroxywybutine; D006147:Guanine; D006899:Mixed Function Oxygenases