Evidence map›Paper›PMID 20619373›Full record

ArticleBiochimica et biophysica acta2010

E. coli DNA associated with isolated Hfq interacts with Hfq's distal surface and C-terminal domain.

Taylor B Updegrove, John J Correia, Roberto Galletto, Wlodzimierz Bujalowski, Roger M Wartell

Open access · greenAbstract read
In one paragraph

Article in Biochimica et biophysica acta, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

40 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Review
  7. Article
  8. Unraveling Membrane Perturbations Caused by the Bacterial Riboregulator Hfq.International journal of molecular sciences · 2022
    Article
  9. Article
  10. Article
  11. The bacterial protein Hfq: Stable modifications and growth phase-dependent changes in SPAM profiles.Journal of chromatography. B, Analytical technologies in the biomedical and life sciences · 2021
    Article
  12. Review
  13. Control ofMicroorganisms · 2020
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  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 at 3 institutions in 1 country.

Taylor B UpdegroveSchool of Biology and Parker H. Petit Institute for Bioscience and Bioengineering, Georgia Institute of Technology, Atlanta, GA 30332, USA.
John J Correia
Roberto Galletto
Wlodzimierz Bujalowski
Roger M Wartell
Georgia Institute of Technology · USThe University of Texas Medical Branch at Galveston · USJackson Memorial Hospital · US

Funding

Functional Dynamics of Mammalian and Viral DNA Repair PolymerasesR01GM058565 · NIGMS · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI BUJALOWSKI, W. M. · 1999 to 2016
$4.6M
THERMODYNAMICS OF PROKARYOTIC DNA REPLICATIONR01GM046679 · NIGMS · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI BUJALOWSKI, W. M. · 1992 to 2012
$3.5M
NIGMS NIH HHS R01 GM046679NIGMS NIH HHS R01 GM058565
6 · The paper itself

Abstract

The RNA-binding protein Hfq has been studied extensively for its function as a modulator of gene expression at the post-transcriptional level. While most Hfq studies have focused on the protein's interaction with sRNAs and mRNAs, Hfq binding to DNA has been observed but is less explored. During the isolation of Hfq from Escherichiacoli, we found genomic DNA fragments associated with the protein after multiple steps of purification. Sequences of 41 amplified segments from the DNA fragments associated with Hfq were determined. A large fraction of the DNA segments were predicted to have significant helical axis curvature and were from genes associated with membrane proteins, characteristics unexpected for non-specific binding. Analysis by analytical ultracentrifugation indicated that rA(18) binding to Hfq disrupts Hfq-DNA interactions. The latter observation suggests Hfq binding to DNA involves its distal surface. This was supported by a gel mobility shift assay that showed single amino acid mutations on the distal surface of Hfq inhibited Hfq binding to duplex DNA, while six of seven mutations on the proximal surface and outer circumference of the hexamer did not prevent Hfq binding. Two mutated Hfq which have portions of their C-terminal domain removed also failed to bind to DNA. The apparent K(d) for binding wild type Hfq to several duplex DNA was estimated from a gel mobility shift assay to be ~400nM.

Indexed as

DNA, BacterialElectrophoretic Mobility Shift AssayEscherichia coliEscherichia coli ProteinsHost Factor 1 ProteinModels, MolecularMutationProtein ConformationProtein Structure, TertiaryUltracentrifugationDNA, BacterialEscherichia coli ProteinsHfq protein, E coliHost Factor 1 Protein

Identifiers

PMID20619373
PMCPMC3072145
OpenAlexW1992505985

What OpenQuestion holds

Textmetadata
LicenceTDM
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.