Evidence map›Paper›PMID 21212119›Full record

ArticleMicrobiology (Reading, England)2011

Ler of pathogenic Escherichia coli forms toroidal protein-DNA complexes.

Jay L Mellies, Gregory Benison, William McNitt, David Mavor, Chris Boniface, Frederick J Larabee

Open access · greenAbstract read
In one paragraph

Article in Microbiology (Reading, England), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

19 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
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  8. Regulation ofEcoSal Plus · 2017
    Review
  9. Review
  10. Review
  11. Article
  12. DNA looping-dependent autorepression of LEE1 P1 promoters by Ler in enteropathogenic Escherichia coli (EPEC).Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
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  15. 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

6 authors at 5 institutions in 1 country.

Jay L MelliesBiology Department, Reed College, Portland, OR 97202, USA.
Gregory BenisonBiology Department, Reed College, Portland, OR 97202, USA.
William McNittCollege of Medicine, University of Oklahoma, Oklahoma City, OK 73104, USA.
David MavorDepartment of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, CA 94143, USA.
Chris BonifaceOregon Health and Sciences University, Portland, OR 97202, USA.
Frederick J LarabeeDepartment of Entomology, University of Illinois Urbana-Champaign, Urbana, IL 61801, USA.
Reed College · USOregon Health & Science University · USUniversity of California, San Francisco · USUniversity of Illinois Urbana-Champaign · USUniversity of Oklahoma · US

Funding

Role of Deamidation in Human Beta-Crystallin StructureR01EY012239 · NEI · OREGON HEALTH & SCIENCE UNIVERSITY · PI LAMPI, KIRSTEN JEANNE · 2004 to 2012
$2.2M
Ler-Mediated Regulation of EPEC Virulence GenesR15AI047802 · NIAID · REED COLLEGE · PI MELLIES, JAY · 2001 to 2008
$607k
DEAMIDATION AND HUMAN BETA CRYSTALLIN STRUCTURER29EY012239 · NEI · OREGON HEALTH AND SCIENCE UNIVERSITY · PI LAMPI, KIRSTEN JEANNE · 1998 to 2002
$433k
NEI NIH HHS EY012239NEI NIH HHS R01 EY012239NEI NIH HHS R29 EY012239NIAID NIH HHS 2 R15 AI047802-03A1NIAID NIH HHS R15 AI047802
6 · The paper itself

Abstract

Enteropathogenic and enterohaemorrhagic Escherichia coli are related pathotypes of bacteria that cause acute watery diarrhoea and haemorrhagic colitis, respectively, and enterohaemorrhagic E. coli can lead to a serious complication known as haemolytic uraemic syndrome. In both bacteria the global regulatory protein Ler controls virulence. The ler gene is found within the locus of enterocyte effacement, or LEE, encoding a type III secretion system necessary for injecting effector proteins into intestinal epithelial cells and causing net secretory diarrhoea. The nucleoid-associated protein H-NS silences, whereas Ler serves as an anti-silencer of, multiple LEE operons. Although Ler has a higher affinity for DNA than does H-NS, the precise molecular mechanism by which Ler increases LEE transcription remains to be determined. In this report we investigate the oligomerization activity of Ler. In solution, Ler forms dimers and soluble aggregates of up to 5000 kDa molecular mass, and appears to oligomerize more readily than the related protein H-NS. An insertional mutation into the Ler linker region diminished oligomerization activity. Despite being proteins of similar mass and having homologous DNA-binding domains, Ler and H-NS complexed to DNA migrated to distinct locations, as determined by an electrophoretic mobility shift assay, implying that the related proteins form different 3D shapes in the presence of DNA. Lastly, we present electron microscopy images of toroidal Ler-DNA structures that are predicted to be involved in stimulating gene expression.

Indexed as

Protein MultimerizationDNA, BacterialElectrophoretic Mobility Shift AssayEscherichia coliEscherichia coli ProteinsMacromolecular SubstancesMicroscopy, ElectronMutagenesis, InsertionalProtein BindingTrans-ActivatorsDNA, BacterialEscherichia coli ProteinsLer protein, E coliMacromolecular SubstancesTrans-Activators

Identifiers

PMID21212119
PMCPMC3139439
OpenAlexW2102045796

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.