Evidence map›Paper›PMID 25701731›Full record

ArticleMicrobiology (Reading, England)2015

Dephosphorylated NPr is involved in an envelope stress response of Escherichia coli.

Jaeseop Lee, Young-Ha Park, Yeon-Ran Kim, Yeong-Jae Seok, Chang-Ro Lee

Open access · greenAbstract read
In one paragraph

Article in Microbiology (Reading, England), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

12 citing papers in PubMed, 24 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Why Nature Chose Potassium.Journal of molecular evolution · 2019
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Structure of the NPr:EINStructure (London, England : 1993) · 2016
    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

5 authors at 2 institutions in 1 country.

Jaeseop LeeDepartment of Biological Sciences, Myongji University, Yongin, Gyeonggido 449-728, Republic of Korea.
Young-Ha ParkDepartment of Biological Sciences and Institute of Microbiology, Seoul National University, Seoul 151-742, Republic of Korea.
Yeon-Ran KimDepartment of Biological Sciences and Institute of Microbiology, Seoul National University, Seoul 151-742, Republic of Korea.
Yeong-Jae SeokDepartment of Biophysics and Chemical Biology, Seoul National University, Seoul 151-742, Republic of Korea.
Chang-Ro LeeDepartment of Biological Sciences, Myongji University, Yongin, Gyeonggido 449-728, Republic of Korea.
Seoul National University · KRMyongji University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Besides the canonical phosphoenolpyruvate-dependent phosphotransferase system (PTS) for carbohydrate transport, most Proteobacteria possess the so-called nitrogen PTS (PTS(Ntr)) that transfers a phosphate group from phosphoenolpyruvate (PEP) over enzyme I(Ntr) (EI(Ntr)) and NPr to enzyme IIA(Ntr) (EIIA(Ntr)). The PTS(Ntr) lacks membrane-bound components and functions exclusively in a regulatory capacity. While EIIA(Ntr) has been implicated in a variety of cellular processes such as potassium homeostasis, phosphate starvation, nitrogen metabolism, carbon metabolism, regulation of ABC transporters and poly-β-hydroxybutyrate accumulation in many Proteobacteria, the only identified role of NPr is the regulation of biosynthesis of the lipopolysaccharide (LPS) layer by direct interaction with LpxD in Escherichia coli. In this study, we provide another phenotype related to NPr. Several lines of evidence demonstrate that E. coli strains with increased levels of dephosphorylated NPr are sensitive to envelope stresses, such as osmotic, ethanol and SDS stresses, and these phenotypes are independent of LpxD. The C-terminal region of NPr plays an important role in sensitivity to envelope stresses. Thus, our data suggest that the dephospho-form of NPr affects adaptation to envelope stresses through a C-terminus-dependent mechanism.

Indexed as

Stress, PhysiologicalAcyltransferasesCarrier ProteinsCell MembraneEscherichia coliEscherichia coli ProteinsGene ExpressionMutationNitrogenPeriplasmic Binding ProteinsPhenotypePhosphate-Binding ProteinsPhosphoenolpyruvate Sugar Phosphotransferase SystemPhosphorylationacyl-(acyl-carrier-protein)-UDP-N-acetylglucosamine acyltransferaseAcyltransferasesCarrier ProteinsEscherichia coli ProteinsNitrogenNPr protein, E coliosmY protein, E coliPeriplasmic Binding ProteinsPhosphate-Binding ProteinsPhosphoenolpyruvate Sugar Phosphotransferase System

Identifiers

PMID25701731
PMCPMC4635465
OpenAlexW2055011516

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.