Evidence map›Paper›PMID 24668810›Full record

ArticleThe Journal of biological chemistry2014

Locus of enterocyte effacement-encoded regulator (Ler) of pathogenic Escherichia coli competes off histone-like nucleoid-structuring protein (H-NS) through noncooperative DNA binding.

Ricksen S Winardhi, Ranjit Gulvady, Jay L Mellies, Jie Yan

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

23 citing papers in PubMed, 41 citations in OpenAlex.

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  16. Type Three Secretion System in Attaching and Effacing Pathogens.Frontiers in cellular and infection microbiology · 2016
    Review
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  18. Article
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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 at 2 institutions in 2 countries.

Ricksen S WinardhiFrom the NUS Graduate School for Integrative Sciences and Engineering, National University of Singapore, Singapore 117456, Singapore, the Mechanobiology Institute, Singapore 117411, Singapore, the Centre for BioImaging Sciences, National University of Singapore, Singapore 117543, Singapore.
Ranjit Gulvadythe Mechanobiology Institute, Singapore 117411, Singapore, the Centre for BioImaging Sciences, National University of Singapore, Singapore 117543, Singapore.
Jay L Melliesthe Biology Department, Reed College, Portland, Oregon 97202, and jay.mellies@reed.edu.
Jie Yanthe Mechanobiology Institute, Singapore 117411, Singapore, the Centre for BioImaging Sciences, National University of Singapore, Singapore 117543, Singapore, the Department of Physics, National University of Singapore, Singapore 117542, Singapore phyyj@nus.edu.sg.
National University of Singapore · SGReed College · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The locus of enterocyte effacement-encoded regulator (Ler) of enteropathogenic and enterohemorrhagic Escherichia coli (EPEC and EHEC) functions to activate transcription of virulence genes silenced by the histone-like nucleoid-structuring protein (H-NS). Despite its important role in the bacterial gene regulation, the binding mode of Ler to DNA and its mechanism in alleviating genes repressed by H-NS are largely unknown. In this study, we use magnetic tweezers to demonstrate that Ler binds extended DNA through a largely noncooperative process, which results in DNA stiffening and DNA folding depending on protein concentration. We also show that Ler can replace prebound H-NS on DNA over a range of potassium and magnesium concentrations. Our findings reveal the DNA binding properties of Ler and shed light to further understand the anti-silencing activity of Ler.

Indexed as

Binding, CompetitiveBacterial ProteinsDNA, BacterialDNA-Binding ProteinsDose-Response Relationship, DrugEnterohemorrhagic Escherichia coliEnteropathogenic Escherichia coliEscherichia coli ProteinsHydrogen-Ion ConcentrationMagnesium ChlorideNucleic Acid ConformationPotassium ChlorideProtein BindingSubstrate SpecificityTemperatureTrans-ActivatorsBacterial ProteinsDNA, BacterialDNA-Binding ProteinsEscherichia coli ProteinsH-NS protein, bacteriaLer protein, E coliMagnesium ChloridePotassium ChlorideTrans-ActivatorsAtomic Force MicroscopyDNA-binding ProteinGene RegulationH-NSLerMagnetic TweezersProtein-DNA InteractionSingle Molecule Biophysics

Identifiers

PMID24668810
PMCPMC4022848
OpenAlexW2037778401

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.