Evidence map›Paper›PMID 23104381›Full record

ArticleNucleic acids research2013

Study of E. coli Hfq's RNA annealing acceleration and duplex destabilization activities using substrates with different GC-contents.

Martina Doetsch, Sabine Stampfl, Boris Fürtig, Mads Beich-Frandsen, Krishna Saxena, Meghan Lybecker, Renée Schroeder

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

13 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Hfq chaperone brings speed dating to bacterial sRNA.Wiley interdisciplinary reviews. RNA · 2018
    Review
  7. Fluorescence reporters for Hfq oligomerization and RNA annealing.Methods in molecular biology (Clifton, N.J.) · 2015
    Article
  8. Article
  9. Identifying and characterizing Hfq-RNA interactions.Methods (San Diego, Calif.) · 2013
    Review
  10. Article
  11. Cycling of RNAs on Hfq.RNA biology · 2013
    Review
  12. Article
  13. 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

7 authors at 3 institutions in 3 countries.

Martina DoetschDepartment for Biochemistry, Max F Perutz Laboratories, Dr-Bohrgasse 9, 1030 Vienna, Austria.
Sabine Stampfl
Boris Fürtig
Mads Beich-Frandsen
Krishna Saxena
Meghan Lybecker
Renée Schroeder
Goethe University Frankfurt · DEMax Perutz Labs · ATFord Motor Company (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Folding of RNA molecules into their functional three-dimensional structures is often supported by RNA chaperones, some of which can catalyse the two elementary reactions helix disruption and helix formation. Hfq is one such RNA chaperone, but its strand displacement activity is controversial. Whereas some groups found Hfq to destabilize secondary structures, others did not observe such an activity with their RNA substrates. We studied Hfq's activities using a set of short RNAs of different thermodynamic stabilities (GC-contents from 4.8% to 61.9%), but constant length. We show that Hfq's strand displacement as well as its annealing activity are strongly dependent on the substrate's GC-content. However, this is due to Hfq's preferred binding of AU-rich sequences and not to the substrate's thermodynamic stability. Importantly, Hfq catalyses both annealing and strand displacement with comparable rates for different substrates, hinting at RNA strand diffusion and annealing nucleation being rate-limiting for both reactions. Hfq's strand displacement activity is a result of the thermodynamic destabilization of the RNA through preferred single-strand binding whereas annealing acceleration is independent from Hfq's thermodynamic influence. Therefore, the two apparently disparate activities annealing acceleration and duplex destabilization are not in energetic conflict with each other.

Indexed as

Base CompositionCytosineEscherichia coli ProteinsGuanineHost Factor 1 ProteinPeptidesRNARNA, Double-StrandedRNA Foldingtat Gene Products, Human Immunodeficiency VirusThermodynamicsCytosineEscherichia coli ProteinsGuanineHfq protein, E coliHost Factor 1 ProteinPeptidesRNARNA, Double-Strandedtat Gene Products, Human Immunodeficiency Virus

Identifiers

PMID23104381
PMCPMC3592463
OpenAlexW2167615588

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.