Evidence map›Paper›PMID 27551070›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Structural basis for the CsrA-dependent modulation of translation initiation by an ancient regulatory protein.

Florian Altegoer, Stefan A Rensing, Gert Bange

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

26 citing papers in PubMed, 38 citations in OpenAlex.

  1. Bacterial small regulatory RNAs.Nature reviews. Microbiology · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. FlaG competes with FliS-flagellin complexes for access to FlhA in the flagellar T3SS to controlProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  6. Article
  7. Small proteins in Gram-positive bacteria.FEMS microbiology reviews · 2023
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Binding ofFrontiers in microbiology · 2020
    Article
  15. Intermolecular Communication inFrontiers in molecular biosciences · 2020
    Review
  16. Review
  17. Article
  18. Review
  19. Article
  20. RNA Binding by theFrontiers in microbiology · 2019
    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

3 authors at 2 institutions in 1 country.

Florian AltegoerLOEWE Center for Synthetic Microbiology, Department of Chemistry, Philipps University Marburg, 35043 Marburg, Germany; gert.bange@synmikro.uni-marburg.de florian.altegoer@synmikro.uni-marburg.de.
Stefan A RensingPlant Cell Biology, Faculty of Biology, Philipps University Marburg, 35043 Marburg, Germany; BIOSS Centre for Biological Signalling Studies, University of Freiburg, 79104 Freiburg, Germany.
Gert BangeLOEWE Center for Synthetic Microbiology, Department of Chemistry, Philipps University Marburg, 35043 Marburg, Germany; gert.bange@synmikro.uni-marburg.de florian.altegoer@synmikro.uni-marburg.de.
Loewe Center for Synthetic Microbiology · DEUniversity of Freiburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Regulation of translation is critical for maintaining cellular protein levels, and thus protein homeostasis. The conserved RNA-binding protein CsrA (also called RsmA; for carbon storage regulator and regulator of secondary metabolism, respectively; hereafter called CsrA) represents a well-characterized example of regulation at the level of translation initiation in bacteria. Binding of a CsrA homodimer to the 5'UTR of an mRNA occludes the Shine-Dalgarno sequence, blocking ribosome access for translation. Small noncoding RNAs (sRNAs) can competitively antagonize CsrA activity by a well-understood mechanism. However, the regulation of CsrA by the protein FliW is just emerging. FliW antagonizes the CsrA-dependent repression of translation of the flagellar filament protein, flagellin. Crystal structures of the FliW monomer reveal a novel, minimal β-barrel-like fold. Structural analysis of the CsrA/FliW heterotetramer shows that FliW interacts with a C-terminal extension of CsrA. In contrast to the competitive regulation of CsrA by sRNAs, FliW allosterically antagonizes CsrA in a noncompetitive manner by excluding the 5'UTR from the CsrA-RNA binding site. Our phylogenetic analysis shows that the FliW-mediated regulation of CsrA regulation is the ancestral state in flagellated bacteria. We thus demonstrate fundamental mechanistic differences in the regulation of CsrA by sRNA in comparison with an ancient regulatory protein.

Indexed as

Peptide Chain Initiation, TranslationalAllosteric RegulationAmino Acid MotifsBacillus subtilisBinding SitesCloning, MolecularCrystallography, X-RayEscherichia coliEscherichia coli ProteinsFlagellaFlagellinGene ExpressionGeobacillusModels, MolecularPhylogenyProtein BindingCsrA protein, E coliEscherichia coli ProteinsFlagellinRecombinant ProteinsRepressor ProteinsRNA, BacterialRNA-Binding ProteinscrystallographyCsrAflagellumFliWtranslation

Identifiers

PMID27551070
PMCPMC5018767
OpenAlexW2512333799

What OpenQuestion holds

Textmetadata
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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.