Evidence map›Paper›PMID 24828038›Full record

ArticleNature2014

Structural basis of the non-coding RNA RsmZ acting as a protein sponge.

Olivier Duss, Erich Michel, Maxim Yulikov, Mario Schubert, Gunnar Jeschke, Frédéric H-T Allain

Abstract read
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In one paragraph

Article in Nature, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 100 papers.

0numbers the graph read from it
0cells of the map it votes in
100citing papers in PubMed
10.4field-weighted citation impact, top 1% 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

100 citing papers in PubMed, 203 citations in OpenAlex.

  1. Review
  2. Article
  3. Bacterial small regulatory RNAs.Nature reviews. Microbiology · 2026
    Review
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40 more citing papers are in PubMed but not listed here.

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

6 authors at 1 institution in 1 country.

Olivier DussInstitute of Molecular Biology and Biophysics, ETH Zürich, CH-8093 Zürich, Switzerland.
Erich MichelInstitute of Molecular Biology and Biophysics, ETH Zürich, CH-8093 Zürich, Switzerland.
Maxim YulikovLaboratory of Physical Chemistry, ETH Zürich, CH-8093 Zürich, Switzerland.
Mario SchubertInstitute of Molecular Biology and Biophysics, ETH Zürich, CH-8093 Zürich, Switzerland.
Gunnar JeschkeLaboratory of Physical Chemistry, ETH Zürich, CH-8093 Zürich, Switzerland.
Frédéric H-T AllainInstitute of Molecular Biology and Biophysics, ETH Zürich, CH-8093 Zürich, Switzerland.
ETH Zurich · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

MicroRNA and protein sequestration by non-coding RNAs (ncRNAs) has recently generated much interest. In the bacterial Csr/Rsm system, which is considered to be the most general global post-transcriptional regulatory system responsible for bacterial virulence, ncRNAs such as CsrB or RsmZ activate translation initiation by sequestering homodimeric CsrA-type proteins from the ribosome-binding site of a subset of messenger RNAs. However, the mechanism of ncRNA-mediated protein sequestration is not understood at the molecular level. Here we show for Pseudomonas fluorescens that RsmE protein dimers assemble sequentially, specifically and cooperatively onto the ncRNA RsmZ within a narrow affinity range. This assembly yields two different native ribonucleoprotein structures. Using a powerful combination of nuclear magnetic resonance and electron paramagnetic resonance spectroscopy we elucidate these 70-kilodalton solution structures, thereby revealing the molecular mechanism of the sequestration process and how RsmE binding protects the ncRNA from RNase E degradation. Overall, our findings suggest that RsmZ is well-tuned to sequester, store and release RsmE and therefore can be viewed as an ideal protein 'sponge'.

Indexed as

Protein BindingAnimalsBase SequenceElectron Spin Resonance SpectroscopyEscherichia coliEscherichia coli ProteinsMethyltransferasesModels, BiologicalModels, MolecularMolecular WeightNuclear Magnetic Resonance, BiomolecularNucleic Acid ConformationProtein MultimerizationRibonucleasesRibonucleoproteinsRNA, UntranslatedEscherichia coli ProteinsMethyltransferasesRibonucleasesRibonucleoproteinsRNA, UntranslatedRsmE protein, E coli

Identifiers

PMID24828038
OpenAlexW2013512935

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.