Evidence map›Paper›PMID 25737541›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

Cation-induced kinetic heterogeneity of the intron-exon recognition in single group II introns.

Danny Kowerko, Sebastian L B König, Miriam Skilandat, Daniela Kruschel, Mélodie C A S Hadzic, Lucia Cardo, Roland K O Sigel

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. 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
–field-weighted citation impact
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.

  1. Article
  2. Article
  3. Article
  4. Moderate activity of RNA chaperone maximizes the yield of self-spliced pre-RNA in vivo.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Physics-based all-atom modeling of RNA energetics and structure.Wiley interdisciplinary reviews. RNA · 2017
    Review
  12. Article
  13. Directly measuring single-molecule heterogeneity using force spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  14. Article
  15. Article
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

7 authors.

Danny KowerkoDepartment of Chemistry, University of Zurich, 8057 Zurich, Switzerland.
Sebastian L B KönigDepartment of Chemistry, University of Zurich, 8057 Zurich, Switzerland.
Miriam SkilandatDepartment of Chemistry, University of Zurich, 8057 Zurich, Switzerland.
Daniela KruschelDepartment of Chemistry, University of Zurich, 8057 Zurich, Switzerland.
Mélodie C A S HadzicDepartment of Chemistry, University of Zurich, 8057 Zurich, Switzerland.
Lucia CardoDepartment of Chemistry, University of Zurich, 8057 Zurich, Switzerland.
Roland K O SigelDepartment of Chemistry, University of Zurich, 8057 Zurich, Switzerland roland.sigel@chem.uzh.ch.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

RNA is commonly believed to undergo a number of sequential folding steps before reaching its functional fold, i.e., the global minimum in the free energy landscape. However, there is accumulating evidence that several functional conformations are often in coexistence, corresponding to multiple (local) minima in the folding landscape. Here we use the 5'-exon-intron recognition duplex of a self-splicing ribozyme as a model system to study the influence of Mg(2+) and Ca(2+) on RNA tertiary structure formation. Bulk and single-molecule spectroscopy reveal that near-physiological M(2+) concentrations strongly promote interstrand association. Moreover, the presence of M(2+) leads to pronounced kinetic heterogeneity, suggesting the coexistence of multiple docked and undocked RNA conformations. Heterogeneity is found to decrease at saturating M(2+) concentrations. Using NMR, we locate specific Mg(2+) binding pockets and quantify their affinity toward Mg(2+). Mg(2+) pulse experiments show that M(2+) exchange occurs on the timescale of seconds. This unprecedented combination of NMR and single-molecule Förster resonance energy transfer demonstrates for the first time to our knowledge that a rugged free energy landscape coincides with incomplete occupation of specific M(2+) binding sites at near-physiological M(2+) concentrations. Unconventional kinetics in nucleic acid folding frequently encountered in single-molecule experiments are therefore likely to originate from a spectrum of conformations that differ in the occupation of M(2+) binding sites.

Indexed as

Base SequenceBinding SitesCations, DivalentExonsFluorescence Resonance Energy TransferIntronsKineticsMagnesiumMagnetic Resonance SpectroscopyModels, BiologicalMolecular Sequence DataRNA, CatalyticSaccharomyces cerevisiaeCations, DivalentMagnesiumRNA, Catalyticheterogeneitymetal ionsNMRRNA foldingsmFRET

Identifiers

PMID25737541
PMCPMC4371910

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Registered trials

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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.