Evidence map›Paper›PMID 12644489›Full record

ArticleJournal of bacteriology2003

Architecture of a fur binding site: a comparative analysis.

Jennifer L Lavrrar, Mark A McIntosh

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in Journal of bacteriology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

47 citing papers in PubMed, 94 citations in OpenAlex.

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  11. OProceedings of the National Academy of Sciences of the United States of America · 2017
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  12. Article
  13. The Role of the Regulator Fur in Gene Regulation and Virulence ofFrontiers in cellular and infection microbiology · 2017
    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

2 authors at 1 institution in 1 country.

Jennifer L LavrrarDepartment of Molecular Microbiology and Immunology, University of Missouri-Columbia School of Medicine, Columbia, Missouri 65212, USA.
Mark A McIntosh
University of Missouri · US

Funding

MOLECULAR ASPECTS OF MICROBIAL PATHOGENESIST32AI007276 · NIAID · UNIVERSITY OF MISSOURI-COLUMBIA · PI SMITH, ARNOLD LEE · 1987 to 2001
$312k
RECEPTOR MEDIATED UPTAKE OF IRON COMPLEXES IN BACTERIAR01GM054243 · NIGMS · UNIVERSITY OF MISSOURI-COLUMBIA · PI MCINTOSH, MARK A · 1996 to 1999
–
NIAID NIH HHS 5 T32 AI07276NIAID NIH HHS T32 AI007276NIGMS NIH HHS GM54243
6 · The paper itself

Abstract

Fur is an iron-binding transcriptional repressor that recognizes a 19-bp consensus site of the sequence 5'-GATAATGATAATCATTATC-3'. This site can be defined as three adjacent hexamers of the sequence 5'-GATAAT-3', with the third being slightly imperfect (an F-F-F configuration), or as two hexamers in the forward orientation separated by one base pair from a third hexamer in the reverse orientation (an F-F-x-R configuration). Although Fur can bind synthetic DNA sequences containing the F-F-F arrangement, most natural binding sites are variations of the F-F-x-R arrangement. The studies presented here compared the ability of Fur to recognize synthetic DNA sequences containing two to four adjacent hexamers with binding to sequences containing variations of the F-F-x-R arrangement (including natural operator sequences from the entS and fepB promoter regions of Escherichia coli). Gel retardation assays showed that the F-F-x-R architecture was necessary for high-affinity Fur-DNA interactions and that contiguous hexamers were not recognized as effectively. In addition, the stoichiometry of Fur at each binding site was determined, showing that Fur interacted with its minimal 19-bp binding site as two overlapping dimers. These data confirm the proposed overlapping-dimer binding model, where the unit of interaction with a single Fur dimer is two inverted hexamers separated by a C:G base pair, with two overlapping units comprising the 19-bp consensus binding site required for the high-affinity interaction with two Fur dimers.

Indexed as

Bacterial ProteinsBase PairingBase SequenceBinding SitesDimerizationDNAElectrophoretic Mobility Shift AssayEscherichia coli ProteinsMembrane Transport ProteinsModels, MolecularPeriplasmic ProteinsRepressor ProteinsBacterial ProteinsDNAEscherichia coli ProteinsfepB protein, E coliferric uptake regulating proteins, bacterialMembrane Transport ProteinsPeriplasmic ProteinsRepressor Proteins

Identifiers

PMID12644489
PMCPMC151488
OpenAlexW2104610389

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.