Evidence map›Paper›PMID 21205841›Full record

ArticleRNA (New York, N.Y.)2011

The stoichiometry of the Escherichia coli Hfq protein bound to RNA.

Taylor B Updegrove, John J Correia, Yanfeng Chen, Charles Terry, Roger M Wartell

Abstract read
In one paragraph

Article in RNA (New York, N.Y.), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
–field-weighted citation impact
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

31 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Targeting of somatostatin receptors expressed in blood cells using quantum dots coated with vapreotide.Saudi pharmaceutical journal : SPJ : the official publication of the Saudi Pharmaceutical Society · 2018
    Article
  5. Article
  6. Article
  7. RNA search engines empower the bacterial intranet.Biochemical Society transactions · 2017
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Fluorescence reporters for Hfq oligomerization and RNA annealing.Methods in molecular biology (Clifton, N.J.) · 2015
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Identifying and characterizing Hfq-RNA interactions.Methods (San Diego, Calif.) · 2013
    Review
  18. Hfq binding changes the structure ofRNA (New York, N.Y.) · 2013
    Article
  19. Article
  20. Cycling of RNAs on Hfq.RNA biology · 2013
    Review
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.

Taylor B UpdegroveSchool of Biology, Georgia Institute of Technology, Atlanta, Georgia 30332, USA.
John J Correia
Yanfeng Chen
Charles Terry
Roger M Wartell

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Escherichia coli RNA binding protein Hfq is involved in many aspects of post-transcriptional gene expression. Tight binding of Hfq to polyadenylate sequences at the 3' end of mRNAs influences exonucleolytic degradation, while Hfq binding to small noncoding RNAs (sRNA) and their targeted mRNAs facilitate their hybridization which in turn effects translation. Hfq binding to an A-rich tract in the 5' leader region of the rpoS mRNA and to the sRNA DsrA have been shown to be important for DsrA enhanced translation initiation of this mRNA. The complexes of Hfq-A(18) and Hfq-DsrA provide models for understanding how Hfq interacts with these two RNA sequence/structure motifs. Different methods have reported different values for the stoichiometry of Hfq-A(18) and Hfq-DsrA. In this work, mass spectrometry and analytical ultracentrifugation provide direct evidence that the strong binding mode of the Hfq hexamer (Hfq(6)) for A(18) and domain II of DsrA (DsrA(DII)) involve 1:1 complexes. This stoichiometry was also supported by fluorescence anisotropy and a competition gel mobility shift experiment using wild-type and truncated Hfq. More limited studies of Hfq binding to DsrA as well as to the sRNAs RprA, OxyS, and an 18-nt segment of OxyS were also consistent with 1:1 stoichiometry. Mass spectrometry of cross-linked samples of Hfq(6), A(18), and DsrA(DII) exhibit intensity corresponding to a ternary 1:1:1 complex; however, the small intensity of this peak and fluorescence anisotropy experiments did not provide evidence that this ternary complex is stable in solution.

Indexed as

Electrophoretic Mobility Shift AssayEscherichia coliEscherichia coli ProteinsFluorescence PolarizationHost Factor 1 ProteinMutationProtein BindingRNA, BacterialRNA, Small UntranslatedRNA, UntranslatedSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationUltracentrifugationDsrA RNA, E coliEscherichia coli ProteinsHfq protein, E coliHost Factor 1 ProteinRNA, BacterialRNA, Small UntranslatedRNA, Untranslated

Identifiers

PMID21205841
PMCPMC3039148

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.