ArticleRNA (New York, N.Y.)2012
Recognition of guanosine by dissimilar tRNA methyltransferases.
Article in RNA (New York, N.Y.), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 32 citations in OpenAlex.
- Nicotinamide-Based Covalent Inhibitors of tRNA (mACS medicinal chemistry letters · 2026Article
- Comprehensive post-transcriptional modification profiles in individual Staphylococcus aureus tRNA species.Nucleic acids research · 2026Article
- Novel heterozygous compound TRMT5 mutations associated with combined oxidative phosphorylation deficiency 26 in a Chinese family: a case report.BMC pediatrics · 2022Article
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- MgACS catalysis · 2020Article
- tRNA Methylation Is a Global Determinant of Bacterial Multi-drug Resistance.Cell systems · 2019Article
- Transfer RNA Modification Enzymes from Thermophiles and Their Modified Nucleosides in tRNA.Microorganisms · 2018Review
- Selective terminal methylation of a tRNA wobble base.Nucleic acids research · 2018Article
- Codon-Specific Translation by mFrontiers in genetics · 2018Article
- Transfer RNA methyltransferases with a SpoU-TrmD (SPOUT) fold and their modified nucleosides in tRNA.Biomolecules · 2017Review
- Evolution of tRNAPhe:imG2 methyltransferases involved in the biosynthesis of wyosine derivatives in Archaea.RNA (New York, N.Y.) · 2016Article
- Methyl transfer by substrate signaling from a knotted protein fold.Nature structural & molecular biology · 2016Article
- A novel HSD17B10 mutation impairing the activities of the mitochondrial RNase P complex causes X-linked intractable epilepsy and neurodevelopmental regression.RNA biology · 2016Article
- Single-Turnover Kinetics of Methyl Transfer to tRNA by Methyltransferases.Methods in molecular biology (Clifton, N.J.) · 2016Article
- tRNA recognition by a bacterial tRNA Xm32 modification enzyme from the SPOUT methyltransferase superfamily.Nucleic acids research · 2015Article
- Structural basis for methyl-donor-dependent and sequence-specific binding to tRNA substrates by knotted methyltransferase TrmD.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Maintenance of protein synthesis reading frame by EF-P and m(1)G37-tRNA.Nature communications · 2015Article
- Substrate recognition and modification by the nosiheptide resistance methyltransferase.PloS one · 2015Article
- Kinetic Analysis of tRNA Methyltransferases.Methods in enzymology · 2015Article
- Diversity in mechanism and function of tRNA methyltransferases.RNA biology · 2015Review
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Authors and funding
9 authors at 4 institutions in 3 countries.
Funding
Abstract
Guanosines are important for biological activities through their specific functional groups that are recognized for RNA or protein interactions. One example is recognition of N(1) of G37 in tRNA by S-adenosyl-methionine (AdoMet)-dependent tRNA methyltransferases to synthesize m(1)G37-tRNA, which is essential for translational fidelity in all biological domains. Synthesis of m(1)G37-tRNA is catalyzed by TrmD in bacteria and by Trm5 in eukarya and archaea, using unrelated and dissimilar structural folds. This raises the question of how dissimilar proteins recognize the same guanosine. Here we probe the mechanism of discrimination among functional groups of guanosine by TrmD and Trm5. Guanosine analogs were systematically introduced into tRNA through a combination of chemical and enzymatic synthesis. Single turnover kinetic assays and thermodynamic analysis of the effect of each analog on m(1)G37-tRNA synthesis reveal that TrmD and Trm5 discriminate functional groups differently. While both recognize N(1) and O(6) of G37, TrmD places a much stronger emphasis on these functional groups than Trm5. While the exocyclic 2-amino group of G37 is important for TrmD, it is dispensable for Trm5. In addition, while an adjacent G36 is obligatory for TrmD, it is nonessential for Trm5. These results depict a more rigid requirement of guanosine functional groups for TrmD than for Trm5. However, the sensitivity of both enzymes to analog substitutions, together with an experimental revelation of their low cellular concentrations relative to tRNA substrates, suggests a model in which these enzymes rapidly screen tRNA by direct recognition of G37 in order to monitor the global state of m(1)G37-tRNA.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.