Evidence map›Paper›PMID 24324139›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

HPr antagonizes the anti-σ70 activity of Rsd in Escherichia coli.

Young-Ha Park, Chang-Ro Lee, Mangyu Choe, Yeong-Jae Seok

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

32 citing papers in PubMed, 51 citations in OpenAlex.

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  17. Review
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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 1 country.

Young-Ha ParkDepartment of Biological Sciences and Institute of Microbiology, Seoul National University, Seoul 151-742, Korea.
Chang-Ro Lee
Mangyu Choe
Yeong-Jae Seok
Seoul National University · KRMyongji University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The bacterial phosphoenolpyruvate:sugar phosphotransferase system (PTS) is a multicomponent system that participates in a variety of physiological processes in addition to the phosphorylation-coupled transport of numerous sugars. In Escherichia coli and other enteric bacteria, enzyme IIA(Glc) (EIIA(Glc)) is known as the central processing unit of carbon metabolism and plays multiple roles, including regulation of adenylyl cyclase, the fermentation/respiration switch protein FrsA, glycerol kinase, and several non-PTS transporters, whereas the only known regulatory role of the E. coli histidine-containing phosphocarrier protein HPr is in the activation of glycogen phosphorylase. Because HPr is known to be more abundant than EIIA(Glc) in enteric bacteria, we assumed that there might be more regulatory mechanisms connected with HPr. The ligand fishing experiment in this study identified Rsd, an anti-sigma factor known to complex with σ(70) in stationary-phase cells, as an HPr-binding protein in E. coli. Only the dephosphorylated form of HPr formed a tight complex with Rsd and thereby inhibited complex formation between Rsd and σ(70). Dephosphorylated HPr, but not phosphorylated HPr, antagonized the inhibitory effect of Rsd on σ(70)-dependent transcriptions both in vivo and in vitro, and also influenced the competition between σ(70) and σ(S) for core RNA polymerase in the presence of Rsd. Based on these data, we propose that the anti-σ(70) activity of Rsd is regulated by the phosphorylation state-dependent interaction of HPr with Rsd.

Indexed as

Bacterial ProteinsChromatography, AffinityDNA-Directed RNA PolymerasesElectrophoretic Mobility Shift AssayEscherichia coliEscherichia coli ProteinsGene Expression Regulation, BacterialPhosphoenolpyruvate Sugar Phosphotransferase SystemPhosphorylationPlasmidsReal-Time Polymerase Chain ReactionRepressor ProteinsSigma FactorBacterial ProteinsDNA-Directed RNA PolymerasesEscherichia coli Proteinsphosphocarrier protein HPrPhosphoenolpyruvate Sugar Phosphotransferase SystemRepressor ProteinsRNA polymerase sigma 70Rsd protein, E coliSigma Factorglucose signalingsigma factor competitiontranscriptional regulation

Identifiers

PMID24324139
PMCPMC3876255
OpenAlexW1977280681

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.