Evidence map›Paper›PMID 22661574›Full record

ArticleNucleic acids research2012

Requirement of upstream Hfq-binding (ARN)x elements in glmS and the Hfq C-terminal region for GlmS upregulation by sRNAs GlmZ and GlmY.

Nilshad N Salim, Martha A Faner, Jane A Philip, Andrew L Feig

Abstract read
In one paragraph

Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing 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

37 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. 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
  9. Article
  10. Article
  11. Hfq chaperone brings speed dating to bacterial sRNA.Wiley interdisciplinary reviews. RNA · 2018
    Review
  12. Article
  13. Article
  14. C-terminal domain of the RNA chaperone Hfq drives sRNA competition and release of target RNA.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. How do base-pairing small RNAs evolve?FEMS microbiology reviews · 2015
    Review
  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

4 authors.

Nilshad N SalimDepartment of Chemistry, Wayne State University, Detroit, MI 48202, USA.
Martha A Faner
Jane A Philip
Andrew L Feig

Funding

Investigations of Hfq-RNA InteractionsR01GM075068 · NIGMS · WAYNE STATE UNIVERSITY · PI FEIG, ANDREW L · 2005 to 2008
$931k
NIGMS NIH HHS GM075068
6 · The paper itself

Abstract

Hfq is an important RNA-binding protein that helps bacteria adapt to stress. Its primary function is to promote pairing between trans-acting small non-coding RNAs (sRNAs) and their target mRNAs. Identification of essential Hfq-binding motifs in up-stream regions of rpoS and fhlA led us to ask the question whether these elements are a common occurrence among other Hfq-dependent mRNAs as well. Here, we confirm the presence of a similar (ARN)(x) motif in glmS RNA, a gene controlled by two sRNAs (GlmZ and GlmY) in an Hfq-dependent manner. GlmZ represents a canonical sRNA:mRNA pairing system, whereas GlmY is non-canonical, interfacing with the RNA processing protein YhbJ. We show that glmS interacts with both Hfq-binding surfaces in the absence of sRNAs. Even though two (ARN)(x) motifs are present, using a glmS:gfp fusion system, we determined that only one specific (ARN)(x) element is essential for regulation. Furthermore, we show that residues 66-72 in the C-terminal extension of Escherichia coli Hfq are essential for activation of GlmS expression by GlmY, but not with GlmZ. This result shows that the C-terminal extension of Hfq may be required for some forms of non-canonical sRNA regulation involving ancillary components such as additional RNAs or proteins.

Indexed as

Gene Expression Regulation, BacterialBacterial ProteinsBinding SitesClostridioides difficileClostridium perfringensEscherichia coliEscherichia coli ProteinsGlutamine-Fructose-6-Phosphate Transaminase (Isomerizing)Host Factor 1 ProteinNucleic Acid ConformationNucleotide MotifsProtein BiosynthesisRNA, MessengerRNA, Small UntranslatedUp-RegulationBacterial ProteinsEscherichia coli ProteinsGlutamine-Fructose-6-Phosphate Transaminase (Isomerizing)Hfq protein, E coliHost Factor 1 ProteinRNA, MessengerRNA, Small Untranslated

Identifiers

PMID22661574
PMCPMC3439879

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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.