Evidence map›Paper›PMID 23275550›Full record

ArticleNucleic acids research2013

The structural stabilization of the κ three-way junction by Mg(II) represents the first step in the folding of a group II intron.

Daniela Donghi, Maria Pechlaner, Cinzia Finazzo, Bernd Knobloch, Roland K O Sigel

Abstract read
In one paragraph

Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed.

  1. Article
  2. Assembly factors chaperone ribosomal RNA folding by isolating helical junctions that are prone to misfolding.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Specific phosphorothioate substitution within domain 6 of a group II intron ribozyme leads to changes in local structure and metal ion binding.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018
    Article
  8. Review
  9. Studying metal ion binding properties of a three-way junction RNA by heteronuclear NMR.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016
    Article
  10. Improving NMR Structures of RNA.Structure (London, England : 1993) · 2016
    Article
  11. Article
  12. Article
  13. Article
  14. Solution structure and metal ion binding sites of the human CPEB3 ribozyme's P4 domain.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014
    Article
  15. Article
  16. Comparison of the π-stacking properties of purine versus pyrimidine residues. Some generalizations regarding selectivity.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014
    Review
  17. Article
  18. Visualizing the ai5γ group IIB intron.Nucleic acids research · 2014
    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

5 authors.

Daniela DonghiInstitute of Inorganic Chemistry, University of Zurich, Winterthurerstrasse 190, CH-8057 Zurich, Switzerland.
Maria Pechlaner
Cinzia Finazzo
Bernd Knobloch
Roland K O Sigel

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Folding of group II introns is characterized by a first slow compaction of domain 1 (D1) followed by the rapid docking of other domains to this scaffold. D1 compaction initiates in a small subregion encompassing the κ and ζ elements. These two tertiary elements are also the major interaction sites with domain 5 to form the catalytic core. Here, we provide the first characterization of the structure adopted at an early folding step and show that the folding control element can be narrowed down to the three-way junction with the κ motif. In our nuclear magnetic resonance studies of this substructure derived from the yeast mitochondrial group II intron Sc.ai5γ, we show that a high affinity Mg(II) ion stabilizes the κ element and enables coaxial stacking between helices d' and d'', favoring a rigid duplex across the three-way junction. The κ-element folds into a stable GAAA-tetraloop motif and engages in A-minor interactions with helix d'. The addition of cobalt(III)hexammine reveals three distinct binding sites. The Mg(II)-promoted structural rearrangement and rigidification of the D1 core can be identified as the first micro-step of D1 folding.

Indexed as

IntronsBase SequenceBinding SitesCobaltMagnesiumModels, MolecularMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularNucleic Acid ConformationProtonsRNA FoldingCobaltcobalt ammonium complexMagnesiumProtons

Identifiers

PMID23275550
PMCPMC3575829

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.