ArticleRNA (New York, N.Y.)2012
Kinetics of tRNA folding monitored by aminoacylation.
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 23 papers.
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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
23 citing papers in PubMed, 39 citations in OpenAlex.
- Structure-Based Simulations for Folding of a tRNA Isodecoder.Molecules (Basel, Switzerland) · 2026Article
- Analysis of tRNA Aminoacylation by Northern Blotting and Multiplex Small RNA-Seq.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Post-transcriptional methylation of mitochondrial-tRNA differentially contributes to mitochondrial pathology.Nature communications · 2024Article
- RNA modifying enzymes shape tRNA biogenesis and function.The Journal of biological chemistry · 2024Review
- Modifications in the T arm of tRNA globally determine tRNA maturation, function, and cellular fitness.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Structured 3' UTRs destabilize mRNAs in plants.Genome biology · 2024Article
- RNA architecture influences plant biology.Journal of experimental botany · 2021Review
- TheRNA (New York, N.Y.) · 2020Article
- The methyltransferase TrmA facilitates tRNA folding through interaction with its RNA-binding domain.Nucleic acids research · 2020Article
- RNA structure drives interaction with proteins.Nature communications · 2019Article
- Structural, functional and biological insights into the role of Mycobacterium tuberculosis VapBC11 toxin-antitoxin system: targeting a tRNase to tackle mycobacterial adaptation.Nucleic acids research · 2018Article
- Small but large enough: structural properties of armless mitochondrial tRNAs from the nematode Romanomermis culicivorax.Nucleic acids research · 2018Article
- Does RNA secondary structure drive translation or vice versa?Nature structural & molecular biology · 2018Article
- Multi-environment fitness landscapes of a tRNA gene.Nature ecology & evolution · 2018Article
- QueF-Like, a Non-Homologous Archaeosine Synthase from the Crenarchaeota.Biomolecules · 2017Article
- RNA modification enzyme TruB is a tRNA chaperone.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Two for the price of one: RNA modification enzymes as chaperones.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- The Conservation and Function of RNA Secondary Structure in Plants.Annual review of plant biology · 2016Review
- Transcriptome-wide measurement of plant RNA secondary structure.Current opinion in plant biology · 2015Review
- Dynamic profiling of double-stranded RNA binding proteins.Nucleic acids research · 2015Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
We describe a strategy for tracking Mg²⁺-initiated folding of ³²P-labeled tRNA molecules to their native structures based on the capacity for aminoacylation by the cognate aminoacyl-tRNA synthetase enzyme. The approach directly links folding to function, paralleling a common strategy used to study the folding of catalytic RNAs. Incubation of unfolded tRNA with magnesium ions, followed by the addition of aminoacyl-tRNA synthetase and further incubation, yields a rapid burst of aminoacyl-tRNA formation corresponding to the prefolded tRNA fraction. A subsequent slower increase in product formation monitors continued folding in the presence of the enzyme. Further analysis reveals the presence of a parallel fraction of tRNA that folds more rapidly than the majority of the population. The application of the approach to study the influence of post-transcriptional modifications in folding of Escherichia coli tRNA₁(Gln) reveals that the modified bases increase the folding rate but do not affect either the equilibrium between properly folded and misfolded states or the folding pathway. This assay allows the use of ³²P-labeled tRNA in integrated studies combining folding, post-transcriptional processing, and aminoacylation reactions.
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Registered trials
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