Evidence map›Paper›PMID 23316047›Full record

ArticleJournal of bacteriology2013

Dominant negative lptE mutation that supports a role for LptE as a plug in the LptD barrel.

Marcin Grabowicz, Jennifer Yeh, Thomas J Silhavy

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
4.2field-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

32 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. The Structure ofInternational journal of molecular sciences · 2020
    Article
  10. Iron is a ligand of SecA-like metal-binding domainsThe Journal of biological chemistry · 2020
    Article
  11. Defects in Efflux (Antimicrobial agents and chemotherapy · 2019
    Article
  12. Article
  13. Targeting the Sugary Armor ofFrontiers in cellular and infection microbiology · 2019
    Review
  14. Review
  15. Article
  16. Article
  17. Insertion of proteins and lipopolysaccharide into the bacterial outer membrane.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017
    Review
  18. Review
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

Marcin GrabowiczDepartment of Molecular Biology, Princeton University, Princeton, New Jersey, USA.
Jennifer Yeh
Thomas J Silhavy
Princeton University · US

Funding

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 GM34821NIGMS NIH HHS R01 GM034821NIGMS NIH HHS R37 GM034821
6 · The paper itself

Abstract

Lipopolysaccharide (LPS) is the major outer leaflet constituent of the Gram-negative outer membrane (OM) bilayer. A bipartite protein complex of LptD and LptE assembles LPS into the OM. It has been established that LptE assists folding and assembly of its β-barrel partner LptD, yet reported biochemical evidence suggested additional LptE functions. Here, we isolated dominant negative lptE mutations, seeking to inform these functions. The lptE14 mutation increased OM permeability to erythromycin, even when the wild-type lptE gene was present. We show that the lptE14 mutation does not cause a defect in either LptD assembly or LPS export. A spontaneous IS1 insertion in secA suppressed lptE14 erythromycin sensitivity by removing the C-terminal SecB-binding domain of SecA. While this suppressor mutation broadly impeded SecB-dependent secretion of preproteins, we show that suppression was a direct and specific consequence of reduced LptD levels in the OM. We suggest that lptE14 causes poor plugging of the LptD β barrel and that a reduction of ineffectively plugged LptD-LptE14 complexes in the OM decreases permeability to erythromycin. Hence, lptE14 supports a proposed plug-and-barrel LptE-LptD arrangement.

Indexed as

Adenosine TriphosphatasesBacterial Outer Membrane ProteinsBacterial ProteinsBiological TransportCell MembraneErythromycinEscherichia coliEscherichia coli ProteinsLipopolysaccharidesMembrane Transport ProteinsMutationProtein BindingProtein Structure, TertiarySecA ProteinsSEC Translocation ChannelsTransposasesAdenosine TriphosphatasesBacterial Outer Membrane ProteinsBacterial ProteinsErythromycinEscherichia coli ProteinsIS1 transposaseLipopolysaccharidesLptD protein, E coliLptE protein, E coliMembrane Transport ProteinsSecA ProteinsSecB protein, BacteriaSEC Translocation ChannelsTransposases

Identifiers

PMID23316047
PMCPMC3591993
OpenAlexW2009526104

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.