Evidence map›Paper›PMID 24288369›Full record

ArticleNucleic acids research2014

Mapping Hfq-RNA interaction surfaces using tryptophan fluorescence quenching.

Kirsten E Robinson, Jillian Orans, Alexander R Kovach, Todd M Link, Richard G Brennan

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
4.0field-weighted citation impact, top 5% 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

52 citing papers in PubMed, 82 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. What makes a small RNA work?Nucleic acids research · 2025
    Review
  5. Article
  6. Article
  7. Article
  8. An acetyltranferase moonlights as a regulator of the RNA binding repertoire of the RNA chaperone Hfq inProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  9. Review
  10. Article
  11. Intrinsically disordered interaction network in an RNA chaperone revealed by native mass spectrometry.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Specific and Global RNA Regulators inInternational journal of molecular sciences · 2021
    Review
  17. Article
  18. Article
  19. 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

5 authors at 2 institutions in 1 country.

Kirsten E RobinsonDepartment of Biochemistry, Duke University, Durham, NC 27710, USA and Department of Biochemistry and Molecular Biology, University of Texas MD Anderson Cancer Center, Houston, TX 77030, USA.
Jillian Orans
Alexander R Kovach
Todd M Link
Richard G Brennan
The University of Texas MD Anderson Cancer Center · USDuke University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hfq is a posttranscriptional riboregulator and RNA chaperone that binds small RNAs and target mRNAs to effect their annealing and message-specific regulation in response to environmental stressors. Structures of Hfq-RNA complexes indicate that U-rich sequences prefer the proximal face and A-rich sequences the distal face; however, the Hfq-binding sites of most RNAs are unknown. Here, we present an Hfq-RNA mapping approach that uses single tryptophan-substituted Hfq proteins, all of which retain the wild-type Hfq structure, and tryptophan fluorescence quenching (TFQ) by proximal RNA binding. TFQ properly identified the respective distal and proximal binding of A15 and U6 RNA to Gram-negative Escherichia coli (Ec) Hfq and the distal face binding of (AA)3A, (AU)3A and (AC)3A to Gram-positive Staphylococcus aureus (Sa) Hfq. The inability of (GU)3G to bind the distal face of Sa Hfq reveals the (R-L)n binding motif is a more restrictive (A-L)n binding motif. Remarkably Hfq from Gram-positive Listeria monocytogenes (Lm) binds (GU)3G on its proximal face. TFQ experiments also revealed the Ec Hfq (A-R-N)n distal face-binding motif should be redefined as an (A-A-N)n binding motif. TFQ data also demonstrated that the 5'-untranslated region of hfq mRNA binds both the proximal and distal faces of Ec Hfq and the unstructured C-terminus.

Indexed as

5' Untranslated RegionsAmino Acid MotifsBinding SitesEscherichia coli ProteinsFluorescenceHost Factor 1 ProteinListeria monocytogenesModels, MolecularMutationProtein BindingRNAStaphylococcus aureusTryptophan5' Untranslated RegionsEscherichia coli ProteinsHfq protein, E coliHost Factor 1 ProteinRNATryptophan

Identifiers

PMID24288369
PMCPMC3936774
OpenAlexW2097422492

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LicenceCC BY-NC
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Registered trials

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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.