Evidence map›Paper›PMID 26350129›Full record

ArticleJournal of bacteriology2016

The KdpD Sensor Kinase of Escherichia coli Responds to Several Distinct Signals To Turn on Expression of the Kdp Transport System.

Wolfgang Epstein

Abstract read
In one paragraph

Article in Journal of bacteriology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
–field-weighted citation impact
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

18 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Genetic Basis ofLife (Basel, Switzerland) · 2023
    Article
  6. Sensor histidine kinasesFrontiers in cellular and infection microbiology · 2023
    Article
  7. Article
  8. The Promoter of the Immune-Modulating GeneInternational journal of molecular sciences · 2022
    Article
  9. Review
  10. Unappreciated Roles for KTrends in microbiology · 2021
    Review
  11. Role of theFrontiers in genetics · 2021
    Article
  12. Article
  13. Article
  14. The KdpFABC complex - KMolecular membrane biology · 2019
    Article
  15. Why Nature Chose Potassium.Journal of molecular evolution · 2019
    Review
  16. Article
  17. Article
  18. Article
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

1 author.

Wolfgang EpsteinDepartment of Molecular Genetics and Cell Biology, University of Chicago, Chicago, Illinois, USA wolfepstein@gmail.com.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

unlabelledKdp, one of three saturable K(+) uptake systems in Escherichia coli, is the system with the highest affinity for K(+) and the only one whose expression is strongly controlled by medium K(+) concentration. Expression is controlled by a two-component system of KdpD, the sensor kinase, and KdpE, the response regulator. There is general agreement that expression occurs when the growth rate of cells begins to become limited by K(+) availability. How K(+) limitation results in expression has been controversial. Studying the roles of the major components of the growth medium shows that KdpD senses at least two distinct signals inside the cell, those of Na(+) and NH4 (+), and it probably senses other monovalent cations in the cell. KdpD does not sense turgor. IMPORTANCE: The expression of the Kdp K(+) transport system of E. coli occurs when cells become limited in their growth rate by the availability of K(+). Cells sense limited K(+) and try to compensate by taking up other monovalent cations, particularly Na(+) and NH4 (+). These cations are sensed in the cytoplasm by the KdpD response regulator, presumably to stimulate its kinase activity. It is shown that KdpD does not sense turgor, as was suggested earlier.

Indexed as

Ammonium CompoundsCarbohydratesCulture MediaEscherichia coliEscherichia coli ProteinsGene Expression Regulation, BacterialGene Expression Regulation, EnzymologicHeat-Shock ProteinsMutationOperonPotassiumProtein KinasesSignal TransductionSodiumThioredoxin-Disulfide ReductaseThioredoxinsAmmonium CompoundsCarbohydratesCulture MediaEscherichia coli ProteinsHeat-Shock ProteinsKdpD protein, E coliPotassiumProtein KinasesSodiumThioredoxin-Disulfide ReductaseThioredoxinsTrxA protein, E coliuniversal stress protein A, E coli

Identifiers

PMID26350129
PMCPMC4751791

What OpenQuestion holds

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Registered trials

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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.