Evidence map›Paper›PMID 17693433›Full record

ArticleNucleic acids research2007

Ligand-induced folding of the thiM TPP riboswitch investigated by a structure-based fluorescence spectroscopic approach.

Kathrin Lang, Renate Rieder, Ronald Micura

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.

0numbers the graph read from it
0cells of the map it votes in
81citing papers in PubMed
6.6field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

81 citing papers in PubMed, 152 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Riboflow: Using Deep Learning to Classify Riboswitches With ∼99% Accuracy.Frontiers in bioengineering and biotechnology · 2020
    Article
  9. Article
  10. Article
  11. Evaluating riboswitch optimality.Methods in enzymology · 2019
    Article
  12. Practical synthesis ofMonatshefte fur chemie · 2019
    Article
  13. Riboswitches and Translation Control.Cold Spring Harbor perspectives in biology · 2018
    Review
  14. Article
  15. Monovalent ions modulate the flux through multiple folding pathways of an RNA pseudoknot.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  16. Article
  17. Single-molecule FRET studies on the cotranscriptional folding of a thiamine pyrophosphate riboswitch.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  18. Article
  19. Article
  20. Review

21 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Kathrin LangInstitute of Organic Chemistry, Center for Molecular Biosciences Innsbruck, Leopold Franzens University, Innrain 52a, 6020 Innsbruck, Austria.
Renate Rieder
Ronald Micura
Universität Innsbruck · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Riboswitches are genetic control elements within non-coding regions of mRNA. They consist of a metabolite-sensitive aptamer and an adjoining expression platform. Here, we describe ligand-induced folding of a thiamine pyrophosphate (TPP) responsive riboswitch from Escherichia coli thiM mRNA, using chemically labeled variants. Referring to a recent structure determination of the TPP/aptamer complex, each variant was synthesized with a single 2-aminopurine (AP) nucleobase replacement that was selected to monitor formation of tertiary interactions of a particular region during ligand binding in real time by fluorescence experiments. We have determined the rate constants for conformational adjustment of the individual AP sensors. From the 7-fold differentiation of these constants, it can be deduced that tertiary contacts between the two parallel helical domains (P2/J3-2/P3/L3 and P4/P5/L5) that grip the ligand's ends in two separate pockets, form significantly faster than the function-critical three-way junction with stem P1 fully developed. Based on these data, we characterize the process of ligand binding by an induced fit of the RNA and propose a folding model of the TPP riboswitch aptamer. For the full-length riboswitch domain and for shorter constructs that represent transcriptional intermediates, we have additionally evaluated ligand-induced folding via AP-modified variants and provide insights into the sequential folding pathway that involves a finely balanced equilibrium of secondary structures.

Indexed as

Regulatory Sequences, Ribonucleic Acid2-Aminopurine3' Untranslated RegionsBase SequenceEscherichia coliKineticsLigandsModels, MolecularMolecular Sequence DataNucleic Acid ConformationRNA, BacterialSpectrometry, FluorescenceThiamine PyrophosphateTranscription, GeneticUntranslated Regions2-Aminopurine3' Untranslated RegionsLigandsRegulatory Sequences, Ribonucleic AcidRNA, BacterialThiamine PyrophosphateUntranslated Regions

Identifiers

PMID17693433
PMCPMC2018614
OpenAlexW2151842147

What OpenQuestion holds

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LicenceCC BY-NC
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Registered trials

None linked

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.