Evidence map›Paper›PMID 26354770›Full record

ArticleRNA (New York, N.Y.)2015

Differential effects of ribosomal proteins and Mg2+ ions on a conformational switch during 30S ribosome 5'-domain assembly.

Sanjaya C Abeysirigunawardena, Sarah A Woodson

Abstract read
In one paragraph

Article in RNA (New York, N.Y.), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Exchange dynamics and kinetic control of gene regulation complexes.Nature reviews. Molecular cell biology · 2026
    Review
  2. Article
  3. Quantifying MgbioRxiv : the preprint server for biology · 2026
    Article
  4. Transient ion-mediated interactions regulate subunit rotation in a eukaryotic ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Adventures with RNA graphs.Methods (San Diego, Calif.) · 2018
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Probing RNA folding pathways by RNA fingerprinting.Current protocols in nucleic acid chemistry · 2001
    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

2 authors.

Sanjaya C AbeysirigunawardenaT.C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, Maryland 21218, USA.
Sarah A WoodsonT.C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, Maryland 21218, USA.

Funding

TIME RESOLVED HYDROXYL RADICAL FOOTPRINTING OF RNAR01GM060819 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI WOODSON, SARAH A. · 1999 to 2019
$6.1M
NIGMS NIH HHS R01 GM060819NIGMS NIH HHS R01 GM60819
6 · The paper itself

Abstract

Ribosomal protein S4 nucleates assembly of the 30S ribosome 5' and central domains, which is crucial for the survival of cells. Protein S4 changes the structure of its 16S rRNA binding site, passing through a non-native intermediate complex before forming native S4-rRNA contacts. Ensemble FRET was used to measure the thermodynamic stability of non-native and native S4 complexes in the presence of Mg(2+) ions and other 5'-domain proteins. Equilibrium titrations of Cy3-labeled 5'-domain RNA with Cy5-labeled protein S4 showed that Mg(2+) ions preferentially stabilize the native S4-rRNA complex. In contrast, ribosomal proteins S20 and S16 act by destabilizing the non-native S4-rRNA complex. The full cooperative switch to the native complex requires S4, S16, and S20 and is achieved to a lesser degree by S4 and S16. The resulting thermodynamic model for assembly of the 30S body illustrates how ribosomal proteins selectively bias the equilibrium between alternative rRNA conformations, increasing the cooperativity of rRNA folding beyond what can be achieved by Mg(2+) ions alone.

Indexed as

Binding SitesEscherichia coliMagnesiumProtein BindingProtein ConformationProtein Structure, TertiaryRibosomal ProteinsRibosomesRNA, RibosomalThermodynamicsMagnesiumRibosomal ProteinsRNA, RibosomalFRETribosomal protein S4ribosome assemblyRNA–protein interactions

Identifiers

PMID26354770
PMCPMC4604426

What OpenQuestion holds

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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.