Evidence map›Paper›PMID 22965117›Full record

ArticleNucleic acids research2012

Structural mechanism of Staphylococcus aureus Hfq binding to an RNA A-tract.

Nicola Horstmann, Jillian Orans, Poul Valentin-Hansen, Samuel A Shelburne, Richard G Brennan

Open access · goldAbstract 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 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

25 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Impacts of Small RNAs and Their Chaperones on Bacterial Pathogenicity.Frontiers in cellular and infection microbiology · 2021
    Review
  8. Article
  9. Article
  10. Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  11. Article
  12. Hfq chaperone brings speed dating to bacterial sRNA.Wiley interdisciplinary reviews. RNA · 2018
    Review
  13. Article
  14. Hfq: the flexible RNA matchmaker.Current opinion in microbiology · 2016
    Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Identifying and characterizing Hfq-RNA interactions.Methods (San Diego, Calif.) · 2013
    Review
  20. RNA-mediated regulation in pathogenic bacteria.Cold Spring Harbor perspectives in medicine · 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 at 3 institutions in 2 countries.

Nicola HorstmannDepartment of Biochemistry and Molecular Biology, UT MD Anderson Cancer Center, Houston, TX 77030, USA.
Jillian Orans
Poul Valentin-Hansen
Samuel A Shelburne
Richard G Brennan
Duke University · USThe University of Texas MD Anderson Cancer Center · USUniversity of Southern Denmark · DK

Funding

Analysis Of Group A Streptococcus-Saliva InteractionK08AI064564 · NIAID · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI SHELBURNE, SAMUEL A · 2006 to 2009
$492k
NIAID NIH HHS K8 AI-064564
6 · The paper itself

Abstract

Hfq is a post-transcriptional regulator that plays a key role in bacterial gene expression by binding AU-rich sequences and A-tracts to facilitate the annealing of sRNAs to target mRNAs and to affect RNA stability. To understand how Hfq from the Gram-positive bacterium Staphylococcus aureus (Sa) binds A-tract RNA, we determined the crystal structure of an Sa Hfq-adenine oligoribonucleotide complex. The structure reveals a bipartite RNA-binding motif on the distal face that is composed of a purine nucleotide-specificity site (R-site) and a non-discriminating linker site (L-site). The (R-L)-binding motif, which is also utilized by Bacillus subtilis Hfq to bind (AG)(3)A, differs from the (A-R-N) tripartite poly(A) RNA-binding motif of Escherichia coli Hfq whereby the Sa Hfq R-site strongly prefers adenosine, is more aromatic and permits deeper insertion of the adenine ring. R-site adenine-stacking residue Phe30, which is conserved among Gram-positive bacterial Hfqs, and an altered conformation about β3 and β4 eliminate the adenosine-specificity site (A-site) and create the L-site. Binding studies show that Sa Hfq binds (AU)(3)A ≈ (AG)(3)A ≥ (AC)(3)A > (AA)(3)A and L-site residue Lys33 plays a significant role. The (R-L) motif is likely utilized by Hfqs from most Gram-positive bacteria to bind alternating (A-N)(n) RNA.

Indexed as

Staphylococcus aureusAmino Acid MotifsGram-Positive BacteriaHost Factor 1 ProteinLysineModels, MolecularPoly AProtein BindingPurinesRNAHost Factor 1 ProteinLysinePoly APurinesRNA

Identifiers

PMID22965117
PMCPMC3505971
OpenAlexW2071924482

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.