F
IPR010386

tRNA-hydroxylase MiaE

InterPro entry
Short nametRNA-Hydrxlase_MiaE
Overlapping
homologous
superfamilies
 
Ferritin-like (IPR012347)

Description

tRNA 2-(methylsulfanyl)-N(6)-isopentenyladenosine(37) hydroxylase (MiaE) is a nonheme diiron monooxygenase that catalyses the posttranscriptional allylic hydroxylation of a modified nucleoside in tRNA called 2-methylthio-N-6-isopentenyl adenosine (ms2i6A). ms2i6A is found at position 37, next to the anticodon at the 3' position in almost all eukaryotic and bacterial tRNA's that read codons beginning with uridine. The miaE gene is absent in Escherichia coli, a finding consistent with the absence of the hydroxylated derivative of ms2i6A in this species
[4, 3, 1, 2]
.

References

1.Steady-state kinetics and spectroscopic characterization of enzyme-tRNA interactions for the non-heme diiron tRNA-monooxygenase, MiaE. Subedi BP, Corder AL, Zhang S, Foss FW Jr, Pierce BS. Biochemistry 54, 363-76, (2015). PMID: 25453905

2.Peroxide-shunt substrate-specificity for the Salmonella typhimurium O2-dependent tRNA modifying monooxygenase (MiaE). Corder AL, Subedi BP, Zhang S, Dark AM, Foss FW Jr, Pierce BS. Biochemistry 52, 6182-96, (2013). PMID: 23906247

3.Isolation of the gene (miaE) encoding the hydroxylase involved in the synthesis of 2-methylthio-cis-ribozeatin in tRNA of Salmonella typhimurium and characterization of mutants. Persson BC, Bjork GR. J. Bacteriol. 175, 7776-85, (1993). View articlePMID: 8253666

4.tRNA-modifying MiaE protein from Salmonella typhimurium is a nonheme diiron monooxygenase. Mathevon C, Pierrel F, Oddou JL, Garcia-Serres R, Blondin G, Latour JM, Menage S, Gambarelli S, Fontecave M, Atta M. Proc. Natl. Acad. Sci. U.S.A. 104, 13295-300, (2007). View articlePMID: 17679698

GO terms

Cross References

This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our Privacy Notice and Terms of Use.