Evidence map›Paper›PMID 17765265›Full record

ArticleJournal of molecular biology2007

Structure and function of the Escherichia coli protein YmgB: a protein critical for biofilm formation and acid-resistance.

Jintae Lee, Rebecca Page, Rodolfo García-Contreras, Jeanne-Marie Palermino, Xue-Song Zhang, Ojus Doshi, Thomas K Wood, Wolfgang Peti

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
3.8field-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

54 citing papers in PubMed, 99 citations in OpenAlex.

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  7. RcsF-independent mechanisms of signaling within the Rcs Phosphorelay.bioRxiv : the preprint server for biology · 2024
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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

8 authors at 2 institutions in 1 country.

Jintae LeeArtie McFerrin Department of Chemical Engineering, Texas A & M University, College Station, TX 77843-3122, USA.
Rebecca Page
Rodolfo García-Contreras
Jeanne-Marie Palermino
Xue-Song Zhang
Ojus Doshi
Thomas K Wood
Wolfgang Peti
Brown University · USTexas A&M University · US

Funding

Plant Biofilm Inhibitors to Discover Biofilm GenesR01EB003872 · NIBIB · TEXAS ENGINEERING EXPERIMENT STATION · PI WOOD, THOMAS K · 2005 to 2008
$1.2M
NIBIB NIH HHS EB 003872-01A1NIBIB NIH HHS R01 EB003872
6 · The paper itself

Abstract

The Escherichia coli gene cluster ymgABC was identified in transcriptome studies to have a role in biofilm development and stability. In this study, we showed that YmgB represses biofilm formation in rich medium containing glucose, decreases cellular motility, and protects the cell from acid indicating that YmgB has a major role in acid-resistance in E. coli. Our data show that these phenotypes are potentially mediated through interactions with the important cell signal indole. In addition, gel mobility-shift assays suggest that YmgB may be a non-specific DNA-binding protein. Using nickel-enrichment DNA microarrays, we showed that YmgB binds, either directly or indirectly, via a probable ligand, genes important for biofilm formation. To advance our understanding of the function of YmgB, we used X-ray crystallography to solve the structure of the protein to 1.8 A resolution. YmgB is a biological dimer that is structurally homologous to the E. coli gene regulatory protein Hha, despite having only 5% sequence identity. This supports our DNA microarray data showing that YmgB is a gene regulatory protein. Therefore, this protein, which clearly has a critical role in acid-resistance in E. coli, has been renamed as AriR for regulator of acid resistance influenced by indole.

Indexed as

BiofilmsProtein Structure, QuaternaryAcidsAmino Acid SequenceCell MovementCrystallography, X-RayDimerizationDNA-Binding ProteinsEscherichia coliEscherichia coli ProteinsHydrogen PeroxideIndolesModels, MolecularMolecular Sequence DataMultigene FamilyOligonucleotide Array Sequence AnalysisAcidsDNA-Binding ProteinsEscherichia coli Proteinshha protein, E coliHydrogen PeroxideIndolesOxidantsThermolysinYmgB protein, E coli

Identifiers

PMID17765265
PMCPMC2185545
OpenAlexW2124576388

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.