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RNA-methyltransferase TrmA is a dual-specific enzyme responsible for C 5 - methylation of uridine in both tmRNA and tRNA

Abstract : In bacteria, trans-translation rescues stalled ribosomes by the combined action of tmRNA (transfer-mRNA) and its associated protein SmpB. The tmRNA 5' and 3' ends fold into a tRNA-like domain (TLD), which shares structural and functional similarities with tRNAs. As in tRNAs, the UUC sequence of the T-arm of the TLD is post-transcriptionally modified to m ( 5) UψC. In tRNAs of gram-negative bacteria, formation of m ( 5) U is catalyzed by the SAM-dependent methyltransferase TrmA, while formation of m ( 5) U at two different positions in rRNA is catalyzed by distinct site-specific methyltransferases RlmC and RlmD. Here, we show that m ( 5) U formation in tmRNAs is exclusively due to TrmA and should be considered as a dual-specific enzyme. The evidence comes from the lack of m ( 5) U in purified tmRNA or TLD variants recovered from an Escherichia coli mutant strain deleted of the trmA gene. Detection of m ( 5) U in RNA was performed by NMR analysis.
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https://hal.archives-ouvertes.fr/hal-02344603
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Ehsan Ranaei-Siadat, Céline Fabret, Bili Seijo, Frédéric Dardel, Henri Grosjean, et al.. RNA-methyltransferase TrmA is a dual-specific enzyme responsible for C 5 - methylation of uridine in both tmRNA and tRNA. RNA Biology, Taylor & Francis, 2014, 10 (4), pp.572-578. ⟨10.4161/rna.24327⟩. ⟨hal-02344603⟩

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