ArticleBiochemistry2017
Capture and Release of tRNA by the T-Loop Receptor in the Function of the T-Box Riboswitch.
Article in Biochemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 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
12 citing papers in PubMed, 18 citations in OpenAlex.
- Structural and dynamic mechanisms for coupled folding and tRNA recognition of a translational T-box riboswitch.Nature communications · 2023Article
- RNA structure determination: From 2D to 3D.Fundamental research · 2023Review
- Recent advances in RNA structurome.Science China. Life sciences · 2022Review
- Towards the Idea of Molecular Brains.International journal of molecular sciences · 2021Review
- Small-Molecule Antibiotics Inhibiting tRNA-Regulated Gene Expression Is a Viable Strategy for Targeting Gram-Positive Bacteria.Antimicrobial agents and chemotherapy · 2020Article
- Structural basis of amino acid surveillance by higher-order tRNA-mRNA interactions.Nature structural & molecular biology · 2019Article
- Long non-coding subgenomic flavivirus RNAs have extended 3D structures and are flexible in solution.EMBO reports · 2019Article
- An evolving tale of two interacting RNAs-themes and variations of the T-box riboswitch mechanism.IUBMB life · 2019Review
- Specific structural elements of the T-box riboswitch drive the two-step binding of the tRNA ligand.eLife · 2018Article
- The T-Box Riboswitch: tRNA as an Effector to Modulate Gene Regulation.Microbiology spectrum · 2018Review
- Hierarchical mechanism of amino acid sensing by the T-box riboswitch.Nature communications · 2018Article
- New tRNA contacts facilitate ligand binding in aProceedings of the National Academy of Sciences of the United States of America · 2018Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
In Gram-positive bacteria, the tRNA-dependent T-box riboswitch system regulates expression of amino acid biosynthetic and aminoacyl-tRNA synthetase genes through a transcription attenuation mechanism. Binding of uncharged tRNA "closes" the switch, allowing transcription read-through. Structural studies of the 100-nucleotide stem I domain reveal tRNA utilizes base pairing and stacking interactions to bind the stem, but little is known structurally about the 180-nucleotide riboswitch core (stem I, stem III, and antiterminator stem) in complex with tRNA or the mechanism of coupling of the intermolecular binding domains crucial to T-box function. Here we utilize solution structural and biophysical methods to characterize the interplay of the different riboswitch-tRNA contact points using Bacillus subtilis and Oceanobacillus iheyensis glycyl T-box and T-box:tRNA constructs. The data reveal that tRNA:riboswitch core binding at equilibrium involves only Specifier-anticodon and antiterminator-acceptor stem pairing. The elbow:platform stacking interaction observed in studies of the T-box stem I domain is released after pairing between the acceptor stem and the bulge in the antiterminator helix. The results are consistent with the model of T-box riboswitch:tRNA function in which tRNA is captured by stem I of the nascent mRNA followed by stabilization of the antiterminator helix and the paused transcription complex.
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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.