"FAD/Folate-Dependent tRNA Methyltransferase: Flavin as a new methyl-transfer agent."
Hamdane D, Argentini M, Cornu D, Golinelli-Pimpaneau B, Fontecave M...
Published 2012-11-18 in J Am Chem Soc .
Pubmed ID: 23157377
DOI identifier: -
|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.|
This publication refers to following proteins:
- TrmFO (Bacillus subtilis)
Last modification of this entry: Nov. 20, 2012