Evidence map›Paper›PMID 23605038›Full record

ArticleNucleic acids research2013

Hfq-bridged ternary complex is important for translation activation of rpoS by DsrA.

Weiwei Wang, Lijun Wang, Jihui Wu, Qingguo Gong, Yunyu Shi

Abstract 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 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

Who cites it

24 citing papers in PubMed.

  1. Journal of molecular biology · 2026
    Article
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  3. Review
  4. Article
  5. Review
  6. Differential Chromosome- and Plasmid-Borne Resistance ofInternational journal of molecular sciences · 2021
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Hfq: the flexible RNA matchmaker.Current opinion in microbiology · 2016
    Review
  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.

Weiwei WangHefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, P R China.
Lijun Wang
Jihui Wu
Qingguo Gong
Yunyu Shi

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The rpoS mRNA, which encodes the master regulator σ(S) of general stress response, requires Hfq-facilitated base pairing with DsrA small RNA for efficient translation at low temperatures. It has recently been proposed that one mechanism underlying Hfq action is to bridge a transient ternary complex by simultaneously binding to rpoS and DsrA. However, no structural evidence of Hfq simultaneously bound to different RNAs has been reported. We detected simultaneous binding of Hfq to rpoS and DsrA fragments. Crystal structures of AU6A•Hfq•A7 and Hfq•A7 complexes were resolved using 1.8- and 1.9-Å resolution, respectively. Ternary complex has been further verified in solution by NMR. In vivo, activation of rpoS translation requires intact Hfq, which is capable of bridging rpoS and DsrA simultaneously into ternary complex. This ternary complex possibly corresponds to a meta-stable transition state in Hfq-facilitated small RNA-mRNA annealing process.

Indexed as

Protein BiosynthesisBacterial ProteinsBinding SitesEscherichia coli ProteinsHost Factor 1 ProteinModels, MolecularRNARNA, MessengerRNA, Small UntranslatedSigma FactorBacterial ProteinsDsrA RNA, E coliEscherichia coli ProteinsHfq protein, E coliHost Factor 1 ProteinRNARNA, MessengerRNA, Small UntranslatedSigma Factorsigma factor KatF protein, Bacteria

Identifiers

PMID23605038
PMCPMC3675490

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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.