ArticleMethods in enzymology2015
Kinetic Analysis of tRNA Methyltransferases.
Article in Methods in enzymology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed, 7 citations in OpenAlex.
- m6A modification is incorporated into bacterial mRNA without specific functional benefit.Nucleic acids research · 2025Article
- Two dynamic N-terminal regions are required for function in ribosomal RNA adenine dimethylase family members.RNA (New York, N.Y.) · 2025Article
- Novel heterozygous compound TRMT5 mutations associated with combined oxidative phosphorylation deficiency 26 in a Chinese family: a case report.BMC pediatrics · 2022Article
- RNA-hydrolyzing activity of metallo-β-lactamase IMP-1.PloS one · 2020Article
- Structural and biochemical analysis of the dual-specificity Trm10 enzyme fromRNA (New York, N.Y.) · 2018Article
- A novel, integrated PET-guided MRS technique resulting in more accurate initial diagnosis of high-grade glioma.The neuroradiology journal · 2016Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Transfer RNA (tRNA) molecules contain many chemical modifications that are introduced after transcription. A major form of these modifications is methyl transfer to bases and backbone groups, using S-adenosyl methionine (AdoMet) as the methyl donor. Each methylation confers a specific advantage to tRNA in structure or in function. A remarkable methylation is to the G37 base on the 3'-side of the anticodon to generate m(1)G37-tRNA, which suppresses frameshift errors during protein synthesis and is therefore essential for cell growth in all three domains of life. This methylation is catalyzed by TrmD in bacteria and by Trm5 in eukaryotes and archaea. Although TrmD and Trm5 catalyze the same methylation reaction, kinetic analysis reveals that these two enzymes are unrelated to each other and are distinct in their reaction mechanism. This chapter summarizes the kinetic assays that are used to reveal the distinction between TrmD and Trm5. Three types of assays are described, the steady-state, the pre-steady-state, and the single-turnover assays, which collectively provide the basis for mechanistic investigation of AdoMet-dependent methyl transfer reactions.
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Registered trials
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