ArticleChemical biology & drug design2016
Identification of Spermidine Binding Site in T-box Riboswitch Antiterminator RNA.
Article in Chemical biology & drug design, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 8 citations in OpenAlex.
- Polycationic Peptides That Bind T-Box Riboswitch Antiterminator RNA and Inhibit Riboswitch Function.Chemical biology & drug design · 2026Article
- Hydroxychloroquine's diverse targets: a new frontier in precision medicine.Frontiers in immunology · 2025Review
- A spermidine riboswitch class in bacteria exploits a close variant of an aptamer for the enzyme cofactor S-adenosylmethionine.Cell reports · 2023Article
- 4-Aminoquinolines modulate RNA structure and function: Pharmacophore implications of a conformationally restricted polyamine.Biochemical and biophysical research communications · 2023Article
- RNA drug discovery: Conformational restriction enhances specific modulation of the T-box riboswitch function.Bioorganic & medicinal chemistry · 2020Article
- Regulation of OmpA Translation and Shigella dysenteriae Virulence by an RNA Thermometer.Infection and immunity · 2020Article
- Structural basis of amino acid surveillance by higher-order tRNA-mRNA interactions.Nature structural & molecular biology · 2019Article
- NMR characterization of RNA small molecule interactions.Methods (San Diego, Calif.) · 2019Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The T-box transcription antitermination riboswitch controls bacterial gene expression by structurally responding to uncharged, cognate tRNA. Previous studies indicated that cofactors, such as the polyamine spermidine, might serve a specific functional role in enhancing riboswitch efficacy. As riboswitch function depends on key RNA structural changes involving the antiterminator element, the interaction of spermidine with the T-box riboswitch antiterminator element was investigated. Spermidine binds antiterminator model RNA with high affinity (micromolar Kd ) based on isothermal titration calorimetry and fluorescence-monitored binding assays. NMR titration studies, molecular modeling, and inline and enzymatic probing studies indicate that spermidine binds at the 3' portion of the highly conserved seven-nucleotide bulge in the antiterminator. Together, these results support the conclusion that spermidine binds the T-box antiterminator RNA preferentially in a location important for antiterminator function. The implications of these findings are significant both for better understanding of the T-box riboswitch mechanism and for antiterminator-targeted drug discovery efforts.
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What OpenQuestion holds
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.