Evidence map›Paper›PMID 28205647›Full record

ArticleScientific reports2017

Microcin PDI regulation and proteolytic cleavage are unique among known microcins.

Zhe Zhao, Lisa H Orfe, Jinxin Liu, Shao-Yeh Lu, Thomas E Besser, Douglas R Call

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
3.1field-weighted citation impact, top 9% 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

13 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Microbiology (Reading, England) · 2023
    Article
  5. Evidence for Widespread Class II Microcins inApplied and environmental microbiology · 2022
    Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. 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

6 authors at 1 institution in 2 countries.

Zhe ZhaoCollege of Oceanography, Hohai University, Nanjing, 210098, P.R.China.
Lisa H OrfePaul G. Allen School for Global Animal Health, Washington State University, Pullman, WA, 99164, USA.
Jinxin LiuPaul G. Allen School for Global Animal Health, Washington State University, Pullman, WA, 99164, USA.
Shao-Yeh LuPaul G. Allen School for Global Animal Health, Washington State University, Pullman, WA, 99164, USA.
Thomas E BesserPaul G. Allen School for Global Animal Health, Washington State University, Pullman, WA, 99164, USA.
Douglas R CallPaul G. Allen School for Global Animal Health, Washington State University, Pullman, WA, 99164, USA.
Washington State University · US

Funding

TRAINING IN BIOTECHNOLOGY: EMPHASIS ON PROTEIN CHEMISTRYT32GM008336 · NIGMS · WASHINGTON STATE UNIVERSITY · PI CALL, DOUGLAS R. · 1989 to 2023
$8.9M
NIGMS NIH HHS T32 GM008336
6 · The paper itself

Abstract

Microcin PDI inhibits a diversity of pathogenic Escherichia coli through the action of an effector protein, McpM. In this study we demonstrated that expression of the inhibitory phenotype is induced under low osmolarity conditions and expression is primarily controlled by the EnvZ/OmpR two-component regulatory system. Functional, mutagenesis and complementation experiments were used to empirically demonstrate that EnvZ is required for the inhibitory phenotype and that regulation of mcpM is dependent on binding of the phosphorylated OmpR to the mcpM promoter region. The phosphorylated OmpR may recognize three different binding sites within this promoter region. Site-directed mutagenesis revealed that the McpM precursor peptide includes two leader peptides that undergo sequential cleavage at positions G17/G18 and G35/A36 during export through the type I secretion system. Competition assays showed that both cleaved products are required for the PDI phenotype although we could not distinguish loss of function from loss of secretion in these assays. McpM has four cysteines within the mature peptide and site-directed mutagenesis experiments demonstrated that the first two cysteines are necessary for McpM to inhibit susceptible cells. Together these data combined with previous work indicate that MccPDI is unique amongst the microcins that have been described to date.

Indexed as

Gene Expression Regulation, BacterialBacterial Outer Membrane ProteinsBacterial ProteinsBacteriocinsBase SequenceBinding SitesEscherichia coliEscherichia coli ProteinsGene Knockout TechniquesGenetic Complementation TestMultienzyme ComplexesPeptide FragmentsPhenotypePhosphorylationPromoter Regions, GeneticProtein BindingBacterial Outer Membrane ProteinsBacterial ProteinsBacteriocinsenvZ protein, E coliEscherichia coli ProteinsmicrocinMultienzyme Complexesosmolarity response regulator proteinsPeptide FragmentsTrans-Activators

Identifiers

PMID28205647
PMCPMC5311971
OpenAlexW2588836132

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.