FAD/folate-dependent tRNA methyltransferase: flavin as a new methyl-transfer agent.


RNAs contain structurally and functionally important modified nucleosides. Methylation, the most frequent RNA modification in all living organisms, mostly relies on SAM (S-adenosylmethionine)-dependent methyltransferases. TrmFO was recently discovered as a unique tRNA methyltransferase using instead methylenetetrahydrofolate and reduced flavin adenine dinucleotide (FAD) as essential cofactors, but its mechanism has remained elusive. Here, we report that TrmFO carries an active tRNA-methylating agent and characterize it as an original enzyme-methylene-FAD covalent adduct by mass spectrometry and a combination of spectroscopic and biochemical methods. Our data support a novel tRNA methylating mechanism.

DOI: 10.1021/ja308145p

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@article{Hamdane2012FADfolatedependentTM, title={FAD/folate-dependent tRNA methyltransferase: flavin as a new methyl-transfer agent.}, author={Djemel Hamdane and Manuela Argentini and David Cornu and B{\'e}atrice Golinelli-Pimpaneau and Marc Fontecave}, journal={Journal of the American Chemical Society}, year={2012}, volume={134 48}, pages={19739-45} }