ArticlePloS one2015
A Faster Triphosphorylation Ribozyme.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 29 citations in OpenAlex.
- A ribozyme ligase that requires a 3' terminal phosphate on its RNA substrate.Nature communications · 2026Article
- Assembly of catalytic complexes from randomized oligonucleotides.Science advances · 2025Article
- Evolution of the substrate specificity of an RNA ligase ribozyme from phosphorimidazole to triphosphate activation.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Peptide conjugates with polyaromatic hydrocarbons can benefit the activity of catalytic RNAs.Chemical science · 2023Article
- A ribozyme that uses lanthanides as cofactor.Nucleic acids research · 2023Article
- On the origin of life: an RNA-focused synthesis and narrative.RNA (New York, N.Y.) · 2023Article
- Prebiotic Chemistry: The Role of Trimetaphosphate in Prebiotic Chemical Evolution.Frontiers in chemistry · 2022Review
- Bacterial Phosphate Granules Contain Cyclic Polyphosphates: Evidence fromJournal of the American Chemical Society · 2020Article
- Prebiotic Chemistry that Could NotLife (Basel, Switzerland) · 2019Article
- Systematic minimization of RNA ligase ribozyme through large-scale design-synthesis-sequence cycles.Nucleic acids research · 2019Article
- Cotranscriptional 3'-End Processing of T7 RNA Polymerase Transcripts by a Smaller HDV Ribozyme.Journal of molecular evolution · 2018Article
- Computational analysis of fitness landscapes and evolutionary networks from in vitro evolution experiments.Methods (San Diego, Calif.) · 2016Article
- Thirty-five years of research into ribozymes and nucleic acid catalysis: where do we stand today?F1000Research · 2016Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In support of the RNA world hypothesis, previous studies identified trimetaphosphate (Tmp) as a plausible energy source for RNA world organisms. In one of these studies, catalytic RNAs (ribozymes) that catalyze the triphosphorylation of RNA 5'-hydroxyl groups using Tmp were obtained by in vitro selection. One ribozyme (TPR1) was analyzed in more detail. TPR1 catalyzes the triphosphorylation reaction to a rate of 0.013 min-1 under selection conditions (50 mM Tmp, 100 mM MgCl2, 22°C). To identify a triphosphorylation ribozyme that catalyzes faster triphosphorylation, and possibly learn about its secondary structure TPR1 was subjected to a doped selection. The resulting ribozyme, TPR1e, contains seven mutations relative to TPR1, displays a previously unidentified duplex that constrains the ribozyme's structure, and reacts at a 24-fold faster rate than the parent ribozyme. Under optimal conditions (150 mM Tmp, 650 mM MgCl2, 40°C), the triphosphorylation rate of TRP1e reaches 6.8 min-1.
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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.