ArticleThe Journal of biological chemistry2012
Characterization and structure of the Aquifex aeolicus protein DUF752: a bacterial tRNA-methyltransferase (MnmC2) functioning without the usually fused oxidase domain (MnmC1).
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 20 citations in OpenAlex.
- Compendium of RNA modifications for bacterial stress adaptation.Microbiology and molecular biology reviews : MMBR · 2026Review
- tRNA modifications in viral replication.The Journal of biological chemistry · 2026Review
- tRNA modifying enzymes MnmE and MnmG are essential forbioRxiv : the preprint server for biology · 2025Article
- Alternate routes to mnmJournal of bacteriology · 2024Article
- Insights into the Mechanism of Installation of 5-Carboxymethylaminomethyl Uridine Hypermodification by tRNA-Modifying Enzymes MnmE and MnmG.Journal of the American Chemical Society · 2023Article
- Identification of a novel 5-aminomethyl-2-thiouridine methyltransferase in tRNA modification.Nucleic acids research · 2023Article
- Cohabitation ofFrontiers in cellular and infection microbiology · 2023Article
- Article
- Transfer RNA Modification Enzymes from Thermophiles and Their Modified Nucleosides in tRNA.Microorganisms · 2018Review
- Bacillus subtilis exhibits MnmC-like tRNA modification activities.RNA biology · 2018Article
- Diverse Mechanisms of Sulfur Decoration in Bacterial tRNA and Their Cellular Functions.Biomolecules · 2017Review
- The output of the tRNA modification pathways controlled by the Escherichia coli MnmEG and MnmC enzymes depends on the growth conditions and the tRNA species.Nucleic acids research · 2014Article
- Modification of the wobble uridine in bacterial and mitochondrial tRNAs reading NNA/NNG triplets of 2-codon boxes.RNA biology · 2014Review
- Methylated nucleosides in tRNA and tRNA methyltransferases.Frontiers in genetics · 2014Review
- Structural basis for hypermodification of the wobble uridine in tRNA by bifunctional enzyme MnmC.BMC structural biology · 2013Article
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Authors and funding
9 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Post-transcriptional modifications of the wobble uridine (U34) of tRNAs play a critical role in reading NNA/G codons belonging to split codon boxes. In a subset of Escherichia coli tRNA, this wobble uridine is modified to 5-methylaminomethyluridine (mnm(5)U34) through sequential enzymatic reactions. Uridine 34 is first converted to 5-carboxymethylaminomethyluridine (cmnm(5)U34) by the MnmE-MnmG enzyme complex. The cmnm(5)U34 is further modified to mnm(5)U by the bifunctional MnmC protein. In the first reaction, the FAD-dependent oxidase domain (MnmC1) converts cmnm(5)U into 5-aminomethyluridine (nm(5)U34), and this reaction is immediately followed by the methylation of the free amino group into mnm(5)U34 by the S-adenosylmethionine-dependent domain (MnmC2). Aquifex aeolicus lacks a bifunctional MnmC protein fusion and instead encodes the Rossmann-fold protein DUF752, which is homologous to the methyltransferase MnmC2 domain of Escherichia coli MnmC (26% identity). Here, we determined the crystal structure of the A. aeolicus DUF752 protein at 2.5 Å resolution, which revealed that it catalyzes the S-adenosylmethionine-dependent methylation of nm(5)U in vitro, to form mnm(5)U34 in tRNA. We also showed that naturally occurring tRNA from A. aeolicus contains the 5-mnm group attached to the C5 atom of U34. Taken together, these results support the recent proposal of an alternative MnmC1-independent shortcut pathway for producing mnm(5)U34 in tRNAs.
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