Evidence map›Paper›PMID 17908933›Full record

ArticleGenes & development2007

Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli.

Joseph G Sklar, Tao Wu, Daniel Kahne, Thomas J Silhavy

Abstract read
In one paragraph

Article in Genes & development, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 278 papers.

0numbers the graph read from it
0cells of the map it votes in
278citing papers in PubMed
–field-weighted citation impact
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

278 citing papers in PubMed.

  1. Review
  2. Article
  3. The mycomembrane proteins PorH and ProtX are inserted at polar growth zones and linked to the cell wall.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. A mechanism for substrate quality control in outer membrane protein assembly.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  11. Article
  12. Review
  13. Applied and environmental microbiology · 2026
    Article
  14. Article
  15. First inhibitor of a bacterial two-partner secretion system.bioRxiv : the preprint server for biology · 2026
    Article
  16. A fluorescent reporter and single-turnover kinetics reveal insight into BAM complex function.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  17. Article
  18. Article
  19. Review
  20. Barrel expansion of outer membrane protein G nanopore through β-hairpin duplication.Protein science : a publication of the Protein Society · 2025
    Article

218 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

4 authors.

Joseph G SklarDepartment of Molecular Biology, Princeton University, Princeton, New Jersey 08544, USA.
Tao Wu
Daniel Kahne
Thomas J Silhavy

Funding

Studies Toward Hybrid Glycopeptide AntibioticsR01GM066174 · NIGMS · PRINCETON UNIVERSITY · PI KAHNE, DANIEL · 2002 to 2018
$8.9M
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 GM66174NIGMS NIH HHS R01 GM034821NIGMS NIH HHS R01 GM066174NIGMS NIH HHS R37 GM034821PHS HHS T32JM07388
6 · The paper itself

Abstract

Integral beta-barrel proteins (OMPs) are a major class of outer membrane proteins in Gram-negative bacteria. In Escherichia coli, these proteins are synthesized in the cytoplasm, translocated across the inner membrane via the Sec machinery, and assembled in the outer membrane through an unknown mechanism that requires the outer membrane YaeT complex and the periplasmic chaperones SurA, DegP, and Skp. Here, we have established the relationship between these three chaperones providing insight into the mechanism of OMP biogenesis using depletion analysis. Depletion of SurA alone results in a marked decrease in outer membrane density, while the loss of DegP and Skp has no effect on outer membrane composition. Furthermore, we demonstrate that SurA and YaeT interact directly in vivo. Based on these results, we suggest that SurA is the primary chaperone responsible for the periplasmic transit of the bulk mass of OMPs to the YaeT complex. The role of Skp and DegP is amplified in the absence of SurA. Evidence presented suggests that DegP/Skp function to rescue OMPs that fall off the SurA pathway. The seemingly redundant periplasmic chaperones do function in parallel, but the relative importance of the primary function of each pathway depends on whether or not cells are under stress.

Indexed as

Bacterial Outer Membrane ProteinsCarrier ProteinsDNA-Binding ProteinsEscherichia coliEscherichia coli ProteinsHeat-Shock ProteinsMolecular ChaperonesPeptidylprolyl IsomerasePeriplasmic ProteinsPorinsProtein FoldingReceptors, VirusSerine EndopeptidasesBacterial Outer Membrane ProteinsBamA protein, E coliCarrier ProteinsDegP proteaseDNA-Binding ProteinsEscherichia coli ProteinsHeat-Shock ProteinsmaltoporinsMolecular ChaperonesOMPA outer membrane proteinsPeptidylprolyl IsomerasePeriplasmic ProteinsPorinsReceptors, VirusSerine EndopeptidasesSkp protein, E coliSurA protein, E coli

Identifiers

PMID17908933
PMCPMC1993877

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.