ArticleNucleic acids research2007
Amino acid residues of the Escherichia coli tRNA(m5U54)methyltransferase (TrmA) critical for stability, covalent binding of tRNA and enzymatic activity.
Article in Nucleic acids research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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21 citing papers in PubMed, 40 citations in OpenAlex.
- Dosa: A method to covalently barcode proteins for high-throughput biochemistry.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- The Rare RNA Methylations m²G, Cm, m⁵U and ms²i⁶A: Roles in Disease Pathogenesis and Emerging Therapeutic Implications.International journal of medical sciences · 2026Review
- Dosa: A method to covalently barcode proteins for high throughput biochemistry.bioRxiv : the preprint server for biology · 2025Article
- 5-Methyluridine is Ubiquitous in Pseudomonas aeruginosa tRNA and Modulates Antimicrobial Resistance and Virulence.Journal of molecular biology · 2025Article
- A robust deep learning approach for identification of RNA 5-methyluridine sites.Scientific reports · 2024Article
- Investigating the mechanism of rough phenotype in a naturally attenuatedFrontiers in medicine · 2024Article
- Human TRMT2A methylates tRNA and contributes to translation fidelity.Nucleic acids research · 2023Article
- m5U-SVM: identification of RNA 5-methyluridine modification sites based on multi-view features of physicochemical features and distributed representation.BMC biology · 2023Article
- Evaluation and development of deep neural networks for RNA 5-Methyluridine classifications using autoBioSeqpy.Frontiers in microbiology · 2023Article
- m5UPred: A Web Server for the Prediction of RNA 5-Methyluridine Sites from Sequences.Molecular therapy. Nucleic acids · 2020Article
- The methyltransferase TrmA facilitates tRNA folding through interaction with its RNA-binding domain.Nucleic acids research · 2020Article
- Chemical tagging for sensitive determination of uridine modifications in RNA.Chemical science · 2020Article
- Transfer RNA Modification Enzymes from Thermophiles and Their Modified Nucleosides in tRNA.Microorganisms · 2018Review
- Insufficient levels of the nrdAB-encoded ribonucleotide reductase underlie the severe growth defect of the Δhda E. coli strain.Molecular microbiology · 2017Article
- Mechanisms of nickel toxicity in microorganisms.Metallomics : integrated biometal science · 2011Review
- Pseudouridine at position 55 in tRNA controls the contents of other modified nucleotides for low-temperature adaptation in the extreme-thermophilic eubacterium Thermus thermophilus.Nucleic acids research · 2011Article
- Stereochemical mechanisms of tRNA methyltransferases.FEBS letters · 2010Review
- N7-Methylguanine at position 46 (m7G46) in tRNA from Thermus thermophilus is required for cell viability at high temperatures through a tRNA modification network.Nucleic acids research · 2010Article
- The crystal structure of Pyrococcus abyssi tRNA (uracil-54, C5)-methyltransferase provides insights into its tRNA specificity.Nucleic acids research · 2008Article
- Structure of a TrmA-RNA complex: A consensus RNA fold contributes to substrate selectivity and catalysis in m5U methyltransferases.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
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3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Escherichia coli trmA gene encodes the tRNA(m5U54)methyltransferase, which catalyses the formation of m5U54 in tRNA. During the synthesis of m5U54, a covalent 62-kDa TrmA-tRNA intermediate is formed between the amino acid C324 of the enzyme and the 6-carbon of uracil. We have analysed the formation of this TrmA-tRNA intermediate and m5U54 in vivo, using mutants with altered TrmA. We show that the amino acids F188, Q190, G220, D299, R302, C324 and E358, conserved in the C-terminal catalytic domain of several RNA(m5U)methyltransferases of the COG2265 family, are important for the formation of the TrmA-tRNA intermediate and/or the enzymatic activity. These amino acids seem to have the same function as the ones present in the catalytic domain of RumA, whose structure is known, and which catalyses the formation of m5U in position 1939 of E. coli 23 S rRNA. We propose that the unusually high in vivo level of the TrmA-tRNA intermediate in wild-type cells may be due to a suboptimal cellular concentration of SAM, which is required to resolve this intermediate. Our results are consistent with the modular evolution of RNA(m5U)methyltransferases, in which the specificity of the enzymatic reaction is achieved by combining the conserved catalytic domain with different RNA-binding domains.
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