Evidence map›Paper›PMID 27282389›Full record

ArticleeLife2016

A lipoprotein/β-barrel complex monitors lipopolysaccharide integrity transducing information across the outer membrane.

Anna Konovalova, Angela M Mitchell, Thomas J Silhavy

Open access · goldAbstract read
In one paragraph

Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing papers in PubMed
5.6field-weighted citation impact, top 4% 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

85 citing papers in PubMed, 108 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Structural and functional insights into the Rcs phosphorelay.bioRxiv : the preprint server for biology · 2026
    Article
  5. Carbapenem-ResistantAntibiotics (Basel, Switzerland) · 2026
    Review
  6. ThemBio · 2026
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Role ofMicroorganisms · 2025
    Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. RcsF-independent mechanisms of signaling within the Rcs Phosphorelay.bioRxiv : the preprint server for biology · 2024
    Article
  20. Signaling through theJournal of bacteriology · 2024
    Article

25 more citing papers are in PubMed but not listed here.

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

3 authors at 1 institution in 1 country.

Anna KonovalovaDepartment of Molecular Biology, Princeton University, Lewis Thomas Laboratory, Princeton, United States.ORCID 0000-0002-2238-8849
Angela M MitchellDepartment of Molecular Biology, Princeton University, Lewis Thomas Laboratory, Princeton, United States.
Thomas J SilhavyDepartment of Molecular Biology, Princeton University, Lewis Thomas Laboratory, Princeton, United States.ORCID 0000-0001-7672-5153
Princeton University · US

Funding

Biogenesis and maintenance of the outer membrane of Gram-negative bacteriaR35GM118024 · NIGMS · PRINCETON UNIVERSITY · PI SILHAVY, THOMAS J. · 2016 to 2025
$8.1M
GENETIC ANALYSIS OF PROTEIN EXPORTR37GM034821 · NIGMS · PRINCETON UNIVERSITY · PI SILHAVY, THOMAS J. · 1999 to 2008
$4.9M
GENETIC ANALYSIS OF PROTEIN EXPORTR01GM034821 · NIGMS · PRINCETON UNIVERSITY · PI SILHAVY, THOMAS J. · 1985 to 2015
$4.7M
NIGMS NIH HHS R01 GM034821NIGMS NIH HHS R35 GM118024NIGMS NIH HHS R37 GM034821
6 · The paper itself

Abstract

Lipoprotein RcsF is the OM component of the Rcs envelope stress response. RcsF exists in complexes with β-barrel proteins (OMPs) allowing it to adopt a transmembrane orientation with a lipidated N-terminal domain on the cell surface and a periplasmic C-terminal domain. Here we report that mutations that remove BamE or alter a residue in the RcsF trans-lumen domain specifically prevent assembly of the interlocked complexes without inactivating either RcsF or the OMP. Using these mutations we demonstrate that these RcsF/OMP complexes are required for sensing OM outer leaflet stress. Using mutations that alter the positively charged surface-exposed domain, we show that RcsF monitors lateral interactions between lipopolysaccharide (LPS) molecules. When these interactions are disrupted by cationic antimicrobial peptides, or by the loss of negatively charged phosphate groups on the LPS molecule, this information is transduced to the RcsF C-terminal signaling domain located in the periplasm to activate the stress response.

Indexed as

Bacterial Outer Membrane ProteinsCell MembraneDNA Mutational AnalysisEscherichia coliEscherichia coli ProteinsLipopolysaccharidesMutant ProteinsBacterial Outer Membrane ProteinsEscherichia coli ProteinsLipopolysaccharidesMutant ProteinsrcsF protein, E coliBam complexCAMPE. coliinfectious diseasemembrane biogenesismicrobiologypolymyxin Bsignal transductionsurface exposed lipoprotein

Identifiers

PMID27282389
PMCPMC4942254
OpenAlexW2413829872

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.