Evidence map›Paper›PMID 31045204›Full record

ArticleNucleic acids research2019

Unprecedented tunability of riboswitch structure and regulatory function by sub-millimolar variations in physiological Mg2.

Kaley McCluskey, Julien Boudreault, Patrick St-Pierre, Cibran Perez-Gonzalez, Adrien Chauvier, Adrien Rizzi, Pascale B Beauregard, Daniel A Lafontaine, J Carlos Penedo

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2019. 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
1.5field-weighted citation impact, top 17% 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, 27 citations in OpenAlex.

  1. Article
  2. Article
  3. Critical Role of MgThe journal of physical chemistry. B · 2025
    Article
  4. Article
  5. SINEUP RNA rescues molecular phenotypes associated with CHD8 suppression in autism spectrum disorder model systems.Molecular therapy : the journal of the American Society of Gene Therapy · 2025
    Article
  6. Journal of bacteriology · 2024
    Article
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  8. Article
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  12. Review
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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 2 institutions in 2 countries.

Kaley McCluskeySUPA School of Physics and Astronomy, University of St. Andrews, Scotland KY16 9SS, UK.
Julien BoudreaultDépartement de Biologie, Université de Sherbrooke, Québec, Canada J1K 2R1.
Patrick St-PierreDépartement de Biologie, Université de Sherbrooke, Québec, Canada J1K 2R1.
Cibran Perez-GonzalezSUPA School of Physics and Astronomy, University of St. Andrews, Scotland KY16 9SS, UK.
Adrien ChauvierDépartement de Biologie, Université de Sherbrooke, Québec, Canada J1K 2R1.
Adrien RizziDépartement de Chimie, Faculté des Sciences, Université de Sherbrooke, Sherbrooke, Canada.
Pascale B BeauregardCentre SÈVE, Département de Biologie, Faculté des Sciences, Université de Sherbrooke, Sherbrooke, Canada.
Daniel A LafontaineDépartement de Biologie, Université de Sherbrooke, Québec, Canada J1K 2R1.
J Carlos PenedoSUPA School of Physics and Astronomy, University of St. Andrews, Scotland KY16 9SS, UK.
Université de Sherbrooke · CAUniversity of St Andrews · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Riboswitches are cis-acting regulatory RNA biosensors that rival the efficiency of those found in proteins. At the heart of their regulatory function is the formation of a highly specific aptamer-ligand complex. Understanding how these RNAs recognize the ligand to regulate gene expression at physiological concentrations of Mg2+ ions and ligand is critical given their broad impact on bacterial gene expression and their potential as antibiotic targets. In this work, we used single-molecule FRET and biochemical techniques to demonstrate that Mg2+ ions act as fine-tuning elements of the amino acid-sensing lysC aptamer's ligand-free structure in the mesophile Bacillus subtilis. Mg2+ interactions with the aptamer produce encounter complexes with strikingly different sensitivities to the ligand in different, yet equally accessible, physiological ionic conditions. Our results demonstrate that the aptamer adapts its structure and folding landscape on a Mg2+-tunable scale to efficiently respond to changes in intracellular lysine of more than two orders of magnitude. The remarkable tunability of the lysC aptamer by sub-millimolar variations in the physiological concentration of Mg2+ ions suggests that some single-aptamer riboswitches have exploited the coupling of cellular levels of ligand and divalent metal ions to tightly control gene expression.

Indexed as

Gene Expression Regulation, BacterialRiboswitchBacillus subtilisFluorescence Resonance Energy TransferLigandsMagnesiumRNA FoldingTranscription, GeneticLigandsMagnesiumRiboswitch

Identifiers

PMID31045204
PMCPMC6614840
OpenAlexW2942798441

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.