Evidence map›Paper›PMID 18155048›Full record

ArticleJournal of molecular biology2008

Assembly of the 5' and 3' minor domains of 16S ribosomal RNA as monitored by tethered probing from ribosomal protein S20.

Laura M Dutca, Gloria M Culver

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

20 citing papers in PubMed, 30 citations in OpenAlex.

  1. Mechanism of 30S subunit recognition and modification by the conserved bacterial ribosomal RNA methyltransferase RsmI.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. International journal of molecular sciences · 2026
    Article
  3. Extraribosomal Functions of Bacterial Ribosomal Proteins-An Update, 2023.International journal of molecular sciences · 2024
    Review
  4. Article
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  10. Structure and dynamics of bacterial ribosome biogenesis.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017
    Review
  11. Article
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  14. Article
  15. Article
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  18. Article
  19. Nob1 binds the single-stranded cleavage site D at the 3'-end of 18S rRNA with its PIN domain.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  20. 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 at 1 institution in 1 country.

Laura M DutcaDepartment of Biochemistry, Biophysics, and Molecular Biology, Iowa State University, Ames, Iowa 50011, USA.
Gloria M Culver
Iowa State University · US

Funding

Assemblying an Understanding of Ribosome BiosynthesisR01GM062432 · NIGMS · UNIVERSITY OF ROCHESTER · PI CULVER, GLORIA M · 2001 to 2018
$5.0M
NIGMS NIH HHS GM62432NIGMS NIH HHS R01 GM062432
6 · The paper itself

Abstract

The ribosomal protein (r-protein) S20 is a primary binding protein. As such, it interacts directly and independently with the 5' domain as well as the 3' minor domain of 16S ribosomal RNA (rRNA) in minimal particles and the fully assembled 30S subunit. The interactions observed between r-protein S20 and the 5' domain of 16S rRNA are quite extensive, while those between r-protein S20 and the 3' minor domain are significantly more limited. In this study, directed hydroxyl radical probing mediated by Fe(II)-derivatized S20 proteins was used to monitor the folding of 16S rRNA during r-protein association and 30S subunit assembly. An analysis of the cleavage patterns in the minimal complexes [16S rRNA and Fe(II)-S20] and the fully assembled 30S subunit containing the same Fe(II)-derivatized proteins shows intriguing similarities and differences. These results suggest that the two domains, 5' and 3' minor, are organized relative to S20 at different stages of assembly. The 5' domain acquires, in a less complex ribonucleoprotein particle than the 3' minor domain, the same architecture as observed in mature subunits. These results are similar to what would be predicted of subunit assembly by the 5'-to-3' direction assembly model.

Indexed as

Escherichia coliEscherichia coli ProteinsFerrous CompoundsHydroxyl RadicalModels, MolecularMutagenesis, Site-DirectedNucleic Acid ConformationProtein BindingRibonucleoproteinsRibosomal ProteinsRibosomesRNA, Ribosomal, 16SEscherichia coli ProteinsFerrous CompoundsHydroxyl RadicalRibonucleoproteinsRibosomal Proteinsribosomal protein S20, E coliRNA, Ribosomal, 16S

Identifiers

PMID18155048
PMCPMC2443948
OpenAlexW2061608924

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.