ArticleRNA biology2015
Identification of determinants for tRNA substrate recognition by Escherichia coli C/U34 2'-O-methyltransferase.
Article in RNA biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed.
- Comprehensive post-transcriptional modification profiles in individual Staphylococcus aureus tRNA species.Nucleic acids research · 2026Article
- RNA modification-mediated multidimensional crosstalk: a novel perspective on gene expression regulation.Genome biology · 2026Review
- A transfer RNA methyltransferase with an unusual domain composition catalyzes 2'-O-methylation at position 6 in tRNA.Nucleic acids research · 2025Article
- Combining Nanopore direct RNA sequencing with genetics and mass spectrometry for analysis of T-loop base modifications across 42 yeast tRNA isoacceptors.Nucleic acids research · 2024Article
- tRNA modifications and tRNA-derived small RNAs: new insights of tRNA in human disease.Cell biology and toxicology · 2024Review
- RNA modifying enzymes shape tRNA biogenesis and function.The Journal of biological chemistry · 2024Review
- A tRNA modification pattern that facilitates interpretation of the genetic code.Frontiers in microbiology · 2024Article
- Diversity in Biological Function and Mechanism of the tRNA Methyltransferase Trm10.Accounts of chemical research · 2023Article
- Different modification pathways for m1A58 incorporation in yeast elongator and initiator tRNAs.Nucleic acids research · 2023Article
- The tRNA identity landscape for aminoacylation and beyond.Nucleic acids research · 2023Review
- Application of mutational profiling: New functional analyses reveal the tRNA recognition mechanism of tRNA mThe Journal of biological chemistry · 2023Article
- Tied up in knots: Untangling substrate recognition by the SPOUT methyltransferases.The Journal of biological chemistry · 2022Review
- ExtracellularRNA (New York, N.Y.) · 2022Article
- New substrates and determinants for tRNA recognition of RNA methyltransferase DNMT2/TRDMT1.RNA biology · 2021Article
- THUMPD3-TRMT112 is a m2G methyltransferase working on a broad range of tRNA substrates.Nucleic acids research · 2021Article
- The occurrence order and cross-talk of different tRNA modifications.Science China. Life sciences · 2021Review
- NAngewandte Chemie (International ed. in English) · 2020Article
- Intellectual disability-associated gene ftsj1 is responsible for 2'-O-methylation of specific tRNAs.EMBO reports · 2020Article
- To be or not to be modified: Miscellaneous aspects influencing nucleotide modifications in tRNAs.IUBMB life · 2019Review
- Regulatory Factors for tRNA Modifications in Extreme- Thermophilic BacteriumFrontiers in genetics · 2019Review
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Post-transcriptional modifications bring chemical diversity to tRNAs, especially at positions 34 and 37 of the anticodon stem-loop (ASL). TrmL is the prokaryotic methyltransferase that catalyzes the transfer of the methyl group from S-adenosyl-L-methionine to the wobble base of tRNA(Leu)CAA and tRNA(Leu)UAA isoacceptors. This Cm34/Um34 modification affects codon-anticodon interactions and is essential for translational fidelity. TrmL-catalyzed 2'-O-methylation requires its homodimerization; however, understanding of the tRNA recognition mechanism by TrmL remains elusive. In the current study, by measuring tRNA methylation by TrmL and performing kinetic analysis of tRNA mutants, we found that TrmL exhibits a fine-tuned tRNA substrate recognition mechanism. Anticodon stem-loop minihelices with an extension of 2 base pairs are the minimal substrate for EcTrmL methylation. A35 is a key residue for TrmL recognition, while A36-A37-A38 are important either via direct interaction with TrmL or due to the necessity for prior isopentenylation (i(6)) at A37. In addition, TrmL only methylates pyrimidines but not purine residues at the wobble position, and the 2'-O-methylation relies on prior N(6)-isopentenyladenosine modification at position 37.
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