Evidence map›Paper›PMID 27626276›Full record

ArticlePloS one2016

DegP Chaperone Suppresses Toxic Inner Membrane Translocation Intermediates.

Esther Braselmann, Julie L Chaney, Matthew M Champion, Patricia L Clark

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.8field-weighted citation impact, top 13% 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

11 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Article
  3. Competing stress-dependent oligomerization pathways regulate self-assembly of the periplasmic protease-chaperone DegP.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  4. Review
  5. Structural characterization of PaFkbA: A periplasmic chaperone fromComputational and structural biotechnology journal · 2021
    Article
  6. Article
  7. Properties of protein unfolded states suggest broad selection for expanded conformational ensembles.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  8. Article
  9. Review
  10. WhiB6 regulation of ESX-1 gene expression is controlled by a negative feedback loop inProceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  11. Transmembrane β-barrels: Evolution, folding and energetics.Biochimica et biophysica acta. Biomembranes · 2017
    Review
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 1 country.

Esther BraselmannDepartment of Chemistry & Biochemistry, University of Notre Dame, Notre Dame, Indiana, United States of America.
Julie L ChaneyDepartment of Chemistry & Biochemistry, University of Notre Dame, Notre Dame, Indiana, United States of America.
Matthew M ChampionDepartment of Chemistry & Biochemistry, University of Notre Dame, Notre Dame, Indiana, United States of America.
Patricia L ClarkDepartment of Chemistry & Biochemistry, University of Notre Dame, Notre Dame, Indiana, United States of America.ORCID http://orcid.org/0000-0001-5462-8248
University of Notre Dame · US

Funding

Chemistry-Biochemistry-Biology Training Program at Notre DameT32GM075762 · NIGMS · UNIVERSITY OF NOTRE DAME · PI CHANG, MAYLAND F, MOBASHERY, SHAHRIAR · 2007 to 2021
$3.7M
OUTER MEMBRANE SECRETION MECHANISM FOR AUTOTRANSPORTER PROTEINSR01GM097573 · NIGMS · UNIVERSITY OF NOTRE DAME · PI CLARK, PATRICIA LOUISE · 2011 to 2014
$1.1M
NIGMS NIH HHS R01 GM097573NIGMS NIH HHS T32 GM075762
6 · The paper itself

Abstract

The periplasm of Gram-negative bacteria includes a variety of molecular chaperones that shepherd the folding and targeting of secreted proteins. A central player of this quality control network is DegP, a protease also suggested to have a chaperone function. We serendipitously discovered that production of the Bordetella pertussis autotransporter virulence protein pertactin is lethal in Escherichia coli ΔdegP strains. We investigated specific contributions of DegP to secretion of pertactin as a model system to test the functions of DegP in vivo. The DegP chaperone activity was sufficient to restore growth during pertactin production. This chaperone dependency could be relieved by changing the pertactin signal sequence: an E. coli signal sequence leading to co-translational inner membrane (IM) translocation was sufficient to suppress lethality in the absence of DegP, whereas an E. coli post-translational signal sequence was sufficient to recapitulate the lethal phenotype. These results identify a novel connection between the DegP chaperone and the mechanism used to translocate a protein across the IM. Lethality coincided with loss of periplasmic proteins, soluble σE, and proteins regulated by this essential stress response. These results suggest post-translational IM translocation can lead to the formation of toxic periplasmic folding intermediates, which DegP can suppress.

Indexed as

Bacterial Outer Membrane ProteinsBacterial Secretion SystemsBlotting, WesternCell MembraneEscherichia coliHeat-Shock ProteinsMass SpectrometryMolecular ChaperonesPeriplasmic ProteinsSerine EndopeptidasesType V Secretion SystemsVirulence Factors, BordetellaBacterial Outer Membrane ProteinsBacterial Secretion SystemsDegP proteaseHeat-Shock ProteinsMolecular ChaperonesPeriplasmic ProteinspertactinSerine EndopeptidasesType V Secretion SystemsVirulence Factors, Bordetella

Identifiers

PMID27626276
PMCPMC5023192
OpenAlexW2520352983

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.