ArticleJournal of biochemistry2014
DNA-rescuable allosteric inhibition of aptamer II ligand affinity by aptamer I element in the shortened Vibrio cholerae glycine riboswitch.
Article in Journal of biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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.
The trial behind it
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
7 citing papers in PubMed.
- Structural basis for Mg²⁺-glycine synergy in the tandem glycine riboswitch revealed by cryo-EM.Npj structural biology · 2026Article
- Visualizing intracellular glycine with two-dye and single-dye ratiometric RNA-based sensors.Nucleic acids research · 2025Article
- Development and characterization of a glycine biosensor system for fine-tuned metabolic regulation in Escherichia coli.Microbial cell factories · 2022Article
- Evaluating riboswitch optimality.Methods in enzymology · 2019Article
- Engineering and characterization of fluorogenic glycine riboswitches.Nucleic acids research · 2016Article
- Review
- Ligand binding by the tandem glycine riboswitch depends on aptamer dimerization but not double ligand occupancy.RNA (New York, N.Y.) · 2014Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Glycine riboswitches contain two aptamers and turn on the expression of downstream genes in bacteria. Although full-length glycine riboswitches were shown to exhibit no glycine-binding cooperativity, the truncated glycine riboswitches were confirmed to bind two glycine molecules cooperatively. Thorough understanding of the ligand-binding cooperativity may shed light on the molecular basis of the cooperativity and help design novel intricate biosensing genetic circuits for application in synthetic biology. A previously proposed sequential model does not readily provide explanation for published data showing a deleterious mutation in the first aptamer inhibiting the glycine binding of the second one. Using the glycine riboswitch from Vibrio cholerae as a model system, we have identified a region in the first aptamer that modulates the second aptamer function especially in the shortened glycine riboswitch. Importantly, this modulation can be rescued by the addition of a complementary oligodeoxynucleotide, demonstrating the feasibility of developing this system into novel genetic circuits that sense both glycine and a DNA signal.
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Registered trials
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