Evidence map›Paper›PMID 21676871›Full record

ArticleThe Journal of biological chemistry2011

Constitutive regulatory activity of an evolutionarily excluded riboswitch variant.

Renaud Tremblay, Jean-François Lemay, Simon Blouin, Jérôme Mulhbacher, Éric Bonneau, Pascale Legault, Paul Dupont, J Carlos Penedo, Daniel A Lafontaine

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

15 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Single-molecule studies of riboswitch folding.Biochimica et biophysica acta · 2014
    Review
  9. Article
  10. Article
  11. Article
  12. Molecular recognition and function of riboswitches.Current opinion in structural biology · 2012
    Review
  13. Article
  14. Article
  15. Review
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

9 authors at 4 institutions in 2 countries.

Renaud TremblayGroupe ARN/RNA Group, Département de Biologie, Faculté des Sciences, Université de Sherbrooke, Québec J1K 2R1, Canada.
Jean-François Lemay
Simon Blouin
Jérôme Mulhbacher
Éric Bonneau
Pascale Legault
Paul Dupont
J Carlos Penedo
Daniel A Lafontaine
Université de Sherbrooke · CAUniversity of St Andrews · GBFonds de Recherche du Québec - Santé · CAUniversité de Montréal · CA

Funding

Canadian Institutes of Health Research MOP-166290Canadian Institutes of Health Research MOP-86502
6 · The paper itself

Abstract

The exquisite specificity of the adenine-responsive riboswitch toward its cognate metabolite has been shown to arise from the formation of a Watson-Crick interaction between the adenine ligand and residue U65. A recent crystal structure of a U65C adenine aptamer variant has provided a rationale for the phylogenetic conservation observed at position 39 for purine aptamers. The G39-C65 variant adopts a compact ligand-free structure in which G39 is accommodated by the ligand binding site and is base-paired to the cytosine at position 65. Here, we demonstrate using a combination of biochemical and biophysical techniques that the G39-C65 base pair not only severely impairs ligand binding but also disrupts the functioning of the riboswitch in vivo by constitutively activating gene expression. Folding studies using single-molecule FRET revealed that the G39-C65 variant displays a low level of dynamic heterogeneity, a feature reminiscent of ligand-bound wild-type complexes. A restricted conformational freedom together with an ability to significantly fold in monovalent ions are exclusive to the G39-C65 variant. This work provides a mechanistic framework to rationalize the evolutionary exclusion of certain nucleotide combinations in favor of sequences that preserve ligand binding and gene regulation functionalities.

Indexed as

Evolution, MolecularAptamers, NucleotideBase Sequencebeta-GalactosidaseDNA PrimersFluorescence Resonance Energy TransferMagnetic Resonance SpectroscopyNucleic Acid ConformationRNATranscription, GeneticAptamers, Nucleotidebeta-GalactosidaseDNA PrimersRNA

Identifiers

PMID21676871
PMCPMC3149334
OpenAlexW1968820055

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.