ArticleBiochemistry2010
Multivector fluorescence analysis of the xpt guanine riboswitch aptamer domain and the conformational role of guanine.
Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 35 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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Who cites it
35 citing papers in PubMed, 61 citations in OpenAlex.
- Harnessing natural RNA triplex elements found in lncRNAs MALAT1 and NEAT1 for engineering of novel riboswitch platforms.Nucleic acids research · 2026Article
- Magnesium ions mitigate metastable states in the regulatory landscape of mRNA elements.RNA (New York, N.Y.) · 2024Article
- A structural intermediate pre-organizes the add adenine riboswitch for ligand recognition.Nucleic acids research · 2021Article
- Ligand Binding Mechanism and Its Relationship with Conformational Changes in Adenine Riboswitch.International journal of molecular sciences · 2020Article
- Article
- Effect of mutations on binding of ligands to guanine riboswitch probed by free energy perturbation and molecular dynamics simulations.Nucleic acids research · 2019Article
- Unprecedented tunability of riboswitch structure and regulatory function by sub-millimolar variations in physiological Mg2.Nucleic acids research · 2019Article
- Monitoring co-transcriptional folding of riboswitches through helicase unwinding.Methods in enzymology · 2019Article
- Life under the Microscope: Single-Molecule Fluorescence Highlights the RNA World.Chemical reviews · 2018Review
- Long-Range Interactions in Riboswitch Control of Gene Expression.Annual review of biophysics · 2017Review
- Ligand-modulated folding of the full-length adenine riboswitch probed by NMR and single-molecule FRET spectroscopy.Nucleic acids research · 2017Article
- Ligand-mediated and tertiary interactions cooperatively stabilize the P1 region in the guanine-sensing riboswitch.PloS one · 2017Article
- Fluorescence-Based Strategies to Investigate the Structure and Dynamics of Aptamer-Ligand Complexes.Frontiers in chemistry · 2016Review
- Predicting RNA 3D structure using a coarse-grain helix-centered model.RNA (New York, N.Y.) · 2015Article
- Ligand binding by the tandem glycine riboswitch depends on aptamer dimerization but not double ligand occupancy.RNA (New York, N.Y.) · 2014Article
- Single-molecule studies of riboswitch folding.Biochimica et biophysica acta · 2014Review
- The purine riboswitch as a model system for exploring RNA biology and chemistry.Biochimica et biophysica acta · 2014Review
- Nanomanipulation of single RNA molecules by optical tweezers.Journal of visualized experiments : JoVE · 2014Article
- Hierarchy of RNA functional dynamics.Annual review of biochemistry · 2014Review
- Riboswitch structure and dynamics by smFRET microscopy.Methods in enzymology · 2014Article
Corrections and comments
- Erratum issued
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Purine riboswitches are RNA regulatory elements that control purine metabolism in response to intracellular concentrations of the purine ligands. Conformational changes of the guanine riboswitch aptamer domain induced by guanine binding lead to transcriptional regulation of genes involved in guanine biosynthesis. The guanine riboswitch aptamer domain has three RNA helices designated P1, P2, and P3. An overall model for the Mg(2+)- and guanine-dependent relative orientations and dynamics of P1, P2, and P3 has not been reported, and the conformational role of guanine under physiologically relevant conditions has not been fully elucidated. In this study, an ensemble and single-molecule fluorescence resonance energy transfer (FRET) study was performed on three orthogonally labeled variants of the xpt guanine riboswitch aptamer domain. The combined FRET data support a model in which the unfolded state of the aptamer domain has a highly dynamic P2 helix that switches rapidly between two orientations relative to nondynamic P1 and P3. At <<1 mM Mg(2+) (in the presence of a saturating level of guanine) or >or=1 mM Mg(2+) (in the absence of guanine), the riboswitch starts to adopt a folded conformation in which loop-loop interactions lock P2 and P3 into place. At >5 mM Mg(2+), further compaction occurs in which P1 more closely approaches P3. Our data help to explain the biological role of guanine as stabilizing the globally folded aptamer domain conformation at physiologically relevant Mg(2+) concentrations (<or=1 mM), whereas in the absence of guanine, much higher Mg(2+) concentrations are required to induce this folding event.
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Registered trials
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.