ArticleProceedings of the National Academy of Sciences of the United States of America2008
Structure of a TrmA-RNA complex: A consensus RNA fold contributes to substrate selectivity and catalysis in m5U methyltransferases.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
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57 citing papers in PubMed, 85 citations in OpenAlex.
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- Recognition of the tRNA structure: Everything everywhere but not all at once.Cell chemical biology · 2024Review
- Human TRMT2A methylates tRNA and contributes to translation fidelity.Nucleic acids research · 2023Article
- Structure, dynamics, and molecular inhibition of the Staphylococcus aureus mThe Journal of biological chemistry · 2022Article
- Structural basis of successive adenosine modifications by the conserved ribosomal methyltransferase KsgA.Nucleic acids research · 2021Article
- Review
- tRNA elbow modifications affect the tRNA pseudouridine synthase TruB and the methyltransferase TrmA.RNA (New York, N.Y.) · 2020Article
- The methyltransferase TrmA facilitates tRNA folding through interaction with its RNA-binding domain.Nucleic acids research · 2020Article
- The hyperthermophilic partners Nanoarchaeum and Ignicoccus stabilize their tRNA T-loops via different but structurally equivalent modifications.Nucleic acids research · 2020Article
- Genome-wide analysis revealed novel molecular features and evolution of Anti-codons in cyanobacterial tRNAs.Saudi journal of biological sciences · 2020Article
- TRMT2B is responsible for both tRNA and rRNA mRNA biology · 2020Article
- Mouse Trmt2B protein is a dual specific mitochondrial metyltransferase responsible for mRNA biology · 2020Article
- Functionally critical residues in the aminoglycoside resistance-associated methyltransferase RmtC play distinct roles in 30S substrate recognition.The Journal of biological chemistry · 2019Article
- FICC-Seq: a method for enzyme-specified profiling of methyl-5-uridine in cellular RNA.Nucleic acids research · 2019Article
- To be or not to be modified: Miscellaneous aspects influencing nucleotide modifications in tRNAs.IUBMB life · 2019Review
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5 authors at 1 institution in 1 country.
Funding
Abstract
TrmA catalyzes S-adenosylmethionine (AdoMet)-dependent methylation of U54 in most tRNAs. We solved the structure of the Escherichia coli 5-methyluridine (m(5)U) 54 tRNA methyltransferase (MTase) TrmA in a covalent complex with a 19-nt T arm analog to 2.4-A resolution. Mutation of the TrmA catalytic base Glu-358 to Gln arrested catalysis and allowed isolation of the covalent TrmA-RNA complex for crystallization. The protein-RNA interface includes 6 nt of the T loop and two proximal base pairs of the stem. U54 is flipped out of the loop into the active site. A58 occupies the space of the everted U54 and is part of a collinear base stack G53-A58-G57-C56-U55. The RNA fold is different from T loop conformations in unbound tRNA or T arm analogs, but nearly identical to the fold of the RNA loop bound at the active site of the m(5)U MTase RumA. In both enzymes, this consensus fold presents the target U and the following two bases to a conserved binding groove on the protein. Outside of this fold, the RumA and TrmA substrates have completely different structures and protein interfaces. Loop residues other than the target U54 make more than half of their hydrogen bonds to the protein via sugar-phosphate moieties, accounting, in part, for the broad consensus sequence for TrmA substrates.
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