Evidence map›Paper›PMID 24722986›Full record

ArticleThe Journal of biological chemistry2014

Assembly of lipopolysaccharide in Escherichia coli requires the essential LapB heat shock protein.

Gracjana Klein, Natalia Kobylak, Buko Lindner, Anna Stupak, Satish Raina

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.

0numbers the graph read from it
0cells of the map it votes in
83citing 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

83 citing papers in PubMed, 107 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Essential Role of LapD in the Absence of Cardiolipins.International journal of molecular sciences · 2026
    Article
  6. Article
  7. Article
  8. Article
  9. NsrR Represses σInternational journal of molecular sciences · 2025
    Article
  10. Article
  11. Article
  12. A periplasmic protein modulates the proteolysis of peptidoglycan hydrolases to maintain cell wall homeostasis inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Dual function of LapB (YciM) in regulatingProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  19. Signaling through theJournal of bacteriology · 2024
    Article
  20. Article

23 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

5 authors at 2 institutions in 2 countries.

Gracjana KleinFrom the Faculty of Chemistry, Gdansk University of Technology, Narutowicza 11/12, 80-233 Gdansk, Poland and the Research Center Borstel, Leibniz-Center for Medicine and Biosciences, Parkallee 22, 23845 Borstel, Germany.
Natalia KobylakFrom the Faculty of Chemistry, Gdansk University of Technology, Narutowicza 11/12, 80-233 Gdansk, Poland and.
Buko Lindnerthe Research Center Borstel, Leibniz-Center for Medicine and Biosciences, Parkallee 22, 23845 Borstel, Germany.
Anna StupakFrom the Faculty of Chemistry, Gdansk University of Technology, Narutowicza 11/12, 80-233 Gdansk, Poland and.
Satish RainaFrom the Faculty of Chemistry, Gdansk University of Technology, Narutowicza 11/12, 80-233 Gdansk, Poland and the Research Center Borstel, Leibniz-Center for Medicine and Biosciences, Parkallee 22, 23845 Borstel, Germany satish.raina@pg.gda.pl.
Gdańsk University of Technology · PLResearch Center Borstel - Leibniz Lung Center · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Here, we describe two new heat shock proteins involved in the assembly of LPS in Escherichia coli, LapA and LapB (lipopolysaccharide assembly protein A and B). lapB mutants were identified based on an increased envelope stress response. Envelope stress-responsive pathways control key steps in LPS biogenesis and respond to defects in the LPS assembly. Accordingly, the LPS content in ΔlapB or Δ(lapA lapB) mutants was elevated, with an enrichment of LPS derivatives with truncations in the core region, some of which were pentaacylated and exhibited carbon chain polymorphism. Further, the levels of LpxC, the enzyme that catalyzes the first committed step of lipid A synthesis, were highly elevated in the Δ(lapA lapB) mutant. Δ(lapA lapB) mutant accumulated extragenic suppressors that mapped either to lpxC, waaC, and gmhA, or to the waaQ operon (LPS biosynthesis) and lpp (Braun's lipoprotein). Increased synthesis of either FabZ (3-R-hydroxymyristoyl acyl carrier protein dehydratase), slrA (novel RpoE-regulated non-coding sRNA), lipoprotein YceK, toxin HicA, or MurA (UDP-N-acetylglucosamine 1-carboxyvinyltransferase) suppressed some of the Δ(lapA lapB) defects. LapB contains six tetratricopeptide repeats and, at the C-terminal end, a rubredoxin-like domain that was found to be essential for its activity. In pull-down experiments, LapA and LapB co-purified with LPS, Lpt proteins, FtsH (protease), DnaK, and DnaJ (chaperones). A specific interaction was also observed between WaaC and LapB. Our data suggest that LapB coordinates assembly of proteins involved in LPS synthesis at the plasma membrane and regulates turnover of LpxC, thereby ensuring balanced biosynthesis of LPS and phospholipids consistent with its essentiality.

Indexed as

HSP70 Heat-Shock ProteinsAmidohydrolasesATP-Dependent ProteasesBase SequenceBlotting, WesternCell MembraneEscherichia coliEscherichia coli ProteinsGene Expression Regulation, BacterialGenes, EssentialGlycosyltransferasesHeat-Shock ProteinsHot TemperatureLipopolysaccharidesMembrane ProteinsModels, MolecularAmidohydrolasesATP-Dependent ProteasesdnaK protein, E coliEscherichia coli ProteinsFtsH protein, E coliGlycosyltransferasesHeat-Shock ProteinsHSP70 Heat-Shock Proteinslipooligosaccharide 1,5-heptosyltransferaseLipopolysaccharidesMembrane ProteinsUDP-3-O-acyl-N-acetylglucosamine deacetylaseYciM protein, E coliEndotoxinGlycobiologyGlycolipid StructureGlycosyltransferasesHeptosyltransferaseLipid ALipopolysaccharide (LPS)MyristoyltransferaseRpoHTetratricopeptide Repeat (TPR)

Identifiers

PMID24722986
PMCPMC4031536
OpenAlexW2039183373

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.