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Nucleic Acids Research 2005 33(13):3955-3964; doi:10.1093/nar/gki703
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Published online 18 July 2005

© The Author 2005. Published by Oxford University Press. All rights reserved
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Article

Identification of a novel gene encoding a flavin-dependent tRNA:m5U methyltransferase in bacteria—evolutionary implications

Jaunius Urbonavicius, Stéphane Skouloubris1, Hannu Myllykallio1 and Henri Grosjean*

CNRS, Enzymology and Structural Biochemistry Laboratory 1 avenue de la Terrasse, F-91198, Gif-sur-Yvette, France 1INSERM Avenir group, Institute of Genetics and Microbiology, CNRS, University Paris XI Orsay, F-91405, France

*To whom correspondence should be addressed. Tel: +33 1 69823468; Fax: +33 1 69823129; Email: henri.grosjean{at}lebs.cnrs-gif.fr

Received May 18, 2005. Revised June 24, 2005. Accepted June 24, 2005.

Formation of 5-methyluridine (ribothymidine) at position 54 of the T-psi loop of tRNA is catalyzed by site-specific tRNA methyltransferases (tRNA:m5U-54 MTase). In all Eukarya and many Gram-negative Bacteria, the methyl donor for this reaction is S-adenosyl-L-methionine (S-AdoMet), while in several Gram-positive Bacteria, the source of carbon is N5, N10-methylenetetrahydrofolate (CH2H4folate). We have identified the gene for Bacillus subtilis tRNA:m5U-54 MTase. The encoded recombinant protein contains tightly bound flavin and is active in Escherichia coli mutant lacking m5U-54 in tRNAs and in vitro using T7 tRNA transcript as substrate. This gene is currently annotated gid in Genome Data Banks and it is here renamed trmFO. TrmFO (Gid) orthologs have also been identified in many other bacterial genomes and comparison of their amino acid sequences reveals that they are phylogenetically distinct from either ThyA or ThyX class of thymidylate synthases, which catalyze folate-dependent formation of deoxyribothymine monophosphate, the universal DNA precursor.

The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors


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