Evidence map›Paper›PMID 19520845›Full record

ArticleThe Journal of biological chemistry2009

3-Hydroxyphenylpropionate and phenylpropionate are synergistic activators of the MhpR transcriptional regulator from Escherichia coli.

Isabel Manso, Begoña Torres, José Manuel Andreu, Margarita Menéndez, Germán Rivas, Carlos Alfonso, Eduardo Díaz, José Luis García, Beatriz Galán

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.2field-weighted citation impact, top 19% 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

15 citing papers in PubMed, 32 citations in OpenAlex.

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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

9 authors at 3 institutions in 1 country.

Isabel MansoDepartamento de Microbiología Molecular, Spain.
Begoña Torres
José Manuel Andreu
Margarita Menéndez
Germán Rivas
Carlos Alfonso
Eduardo Díaz
José Luis García
Beatriz Galán
Centro de Investigaciones Biológicas Margarita Salas · ESConsejo Superior de Investigaciones Científicas · ESInstituto de Química Física Blas Cabrera · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The degradation of the aromatic compound phenylpropionate (PP) in Escherichia coli K-12 requires the activation of two different catabolic pathways coded by the hca and the mhp gene clusters involved in the mineralization of PP and 3-hydroxyphenylpropionate (3HPP), respectively. The compound 3-(2,3-dihydroxyphenyl)propionate (DHPP) is a common intermediate of both pathways which must be cleaved by the MhpB dioxygenase before entering into the primary cell metabolism. Therefore, the degradation of PP has to be controlled by both its specific regulator (HcaR) but also by the MhpR regulator of the mhp cluster. We have demonstrated that 3HPP and DHPP are the true and best activators of MhpR, whereas PP only induces no response. However, in vivo and in vitro transcription experiments have demonstrated that PP activates the MhpR regulator synergistically with the true inducers, representing the first case of such a peculiar synergistic effect described for a bacterial regulator. The three compounds enhanced the interaction of MhpR with its DNA operator in electrophoretic mobility shift assays. Inducer binding to MhpR is detected by circular dichroism and fluorescence spectroscopies. Fluorescence quenching measurements have revealed that the true inducers (3HPP and DHPP) and PP bind with similar affinities and independently to MhpR. This type of dual-metabolite synergy provides great potential for a rapid modulation of gene expression and represents an important feature of transcriptional control. The mhp regulatory system is an example of the high complexity achievable in prokaryotes.

Indexed as

Gene Expression Regulation, BacterialCircular DichroismCluster AnalysisDioxygenasesDose-Response Relationship, DrugEscherichia coliEscherichia coli ProteinsLigandsModels, BiologicalModels, ChemicalModels, GeneticMultigene FamilyPhenylpropionatesSpectrometry, FluorescenceTranscription, Genetic3-carboxyethylcatechol 2,3-dioxygenaseDioxygenasesEscherichia coli ProteinsLigandsPhenylpropionates

Identifiers

PMID19520845
PMCPMC2755845
OpenAlexW2080899318

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.