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TRNA-modifying MiaE protein from Salmonella typhimurium is a nonheme diiron monooxygenase.


ABSTRACT: MiaE catalyzes the posttranscriptional allylic hydroxylation of 2-methylthio-N-6-isopentenyl adenosine in tRNAs. The Salmonella typhimurium enzyme was heterologously expressed in Escherichia coli. The purified enzyme is a monomer with two iron atoms and displays activity in in vitro assays. The type and properties of the iron center were investigated by using a combination of UV-visible absorption, EPR, HYSCORE, and Mössbauer spectroscopies which demonstrated that the MiaE enzyme contains a nonheme dinuclear iron cluster, similar to that found in the hydroxylase component of methane monooxygenase. This is the first example of an enzyme from this important class of diiron monooxygenases to be involved in the hydroxylation of a biological macromolecule and the second example of a redox metalloenzyme participating in tRNA modification.

SUBMITTER: Mathevon C 

PROVIDER: S-EPMC1948905 | biostudies-literature | 2007 Aug

REPOSITORIES: biostudies-literature

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tRNA-modifying MiaE protein from Salmonella typhimurium is a nonheme diiron monooxygenase.

Mathevon Carole C   Pierrel Fabien F   Oddou Jean-Louis JL   Garcia-Serres Ricardo R   Blondin Geneviève G   Latour Jean-Marc JM   Ménage Stéphane S   Gambarelli Serge S   Fontecave Marc M   Atta Mohamed M  

Proceedings of the National Academy of Sciences of the United States of America 20070806 33


MiaE catalyzes the posttranscriptional allylic hydroxylation of 2-methylthio-N-6-isopentenyl adenosine in tRNAs. The Salmonella typhimurium enzyme was heterologously expressed in Escherichia coli. The purified enzyme is a monomer with two iron atoms and displays activity in in vitro assays. The type and properties of the iron center were investigated by using a combination of UV-visible absorption, EPR, HYSCORE, and Mössbauer spectroscopies which demonstrated that the MiaE enzyme contains a nonh  ...[more]

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