Evidence map›Paper›PMID 25937465›Full record

ArticleProgress in biophysics and molecular biology2015

Cytoplasmic sensing by the inner membrane histidine kinase EnvZ.

Yong Hwee Foo, Yunfeng Gao, Hongfang Zhang, Linda J Kenney

Abstract read
In one paragraph

Article in Progress in biophysics and molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
4.0field-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

21 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Histidine kinases and the missing phosphoproteome from prokaryotes to eukaryotes.Laboratory investigation; a journal of technical methods and pathology · 2018
    Review
  11. Article
  12. A New Role of OmpR in Acid and Osmotic Stress inFrontiers in microbiology · 2018
    Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Single cell super-resolution imaging of E. coli OmpR during environmental stress.Integrative biology : quantitative biosciences from nano to macro · 2015
    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

4 authors at 1 institution in 2 countries.

Yong Hwee FooMechanobiology Institute, National University of Singapore, Singapore.
Yunfeng GaoMechanobiology Institute, National University of Singapore, Singapore.
Hongfang ZhangMechanobiology Institute, National University of Singapore, Singapore.
Linda J KenneyMechanobiology Institute, National University of Singapore, Singapore; Jesse Brown Veterans Affairs Medical Center, Chicago, USA; University of Illinois-Chicago, USA. Electronic address: kenneyl@uic.edu.
National University of Singapore · SG

Funding

OmpR and SsrB Regulation of Salmonella VirulenceI01BX000372 · VA · JESSE BROWN VA MEDICAL CENTER · PI KENNEY, LINDA J. · 2009 to 2017
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BLRD VA I01 BX000372
6 · The paper itself

Abstract

Two-component regulatory systems drive signal transduction in bacteria. The simplest of these employs a membrane sensor kinase and a cytoplasmic response regulator. Environmental sensing is typically coupled to gene regulation. The histidine kinase EnvZ and its cognate response regulator OmpR regulate expression of outer membrane proteins (porins) in response to osmotic stress. We used hydrogen:deuterium exchange mass spectrometry to identify conformational changes in the cytoplasmic domain of EnvZ (EnvZc) that were associated with osmosensing. The osmosensor localized to a seventeen amino acid region of the four-helix bundle of the cytoplasmic domain and flanked the His(243) autophosphorylation site. High osmolality increased autophosphorylation of His(243), suggesting that these two events were linked. The transmembrane domains were not required for osmosensing, but mutants in the transmembrane domains altered EnvZ activity. A photoactivatable fusion protein composed of EnvZc fused to the fluorophore mEos2 (EnvZc-mEos2) was as capable as EnvZc in supporting OmpR-dependent ompF and ompC transcription. Over-expression of EnvZc reduced activity, indicating that the EnvZ/OmpR system is not robust. Our results support a model in which osmolytes stabilize helix one in the four-helix bundle of EnvZ by increased hydrogen bonding of the peptide backbone, increasing autophosphorylation and downstream signaling. The likelihood that additional histidine kinases use similar cytoplasmic sensing mechanisms is discussed.

Indexed as

Amino Acid SequenceBacterial Outer Membrane ProteinsBacterial ProteinsBiomechanical PhenomenaCell MembraneCytoplasmEnzyme ActivationEscherichia coliEscherichia coli ProteinsHydrogen-Ion ConcentrationMolecular Sequence DataMultienzyme ComplexesOsmoregulationProtein Structure, TertiaryTrans-ActivatorsBacterial Outer Membrane ProteinsBacterial ProteinsenvZ protein, E coliEscherichia coli ProteinsMultienzyme Complexesosmolarity response regulator proteinsTrans-Activatorshistidine kinasehydrogen:deuterium exchange mass spectrometryOsmoregulationRobustnessSuper-resolution microscopyTwo-component regulatory system EnvZ/OmpR

Identifiers

PMID25937465
PMCPMC5080436
OpenAlexW2074198235

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.