Evidence map›Paper›PMID 15128935›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2004

SecB is a bona fide generalized chaperone in Escherichia coli.

Ronald S Ullers, Joen Luirink, Nellie Harms, Françoise Schwager, Costa Georgopoulos, Pierre Genevaux

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

49 citing papers in PubMed, 116 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. The Functionality of IbpA fromInternational journal of molecular sciences · 2023
    Article
  6. Article
  7. Article
  8. The DisorderedMicroorganisms · 2021
    Article
  9. Redefining Molecular Chaperones as Chaotropes.Frontiers in molecular biosciences · 2021
    Review
  10. Mechanisms of Cotranslational Protein Maturation in Bacteria.Frontiers in molecular biosciences · 2021
    Review
  11. Cotranslational folding of alkaline phosphatase in the periplasm of Escherichia coli.Protein science : a publication of the Protein Society · 2020
    Article
  12. Article
  13. Article
  14. Review
  15. Folding while bound to chaperones.Current opinion in structural biology · 2018
    Review
  16. Article
  17. Directed evolution of SecB chaperones toward toxin-antitoxin systems.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  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

6 authors at 1 institution in 1 country.

Ronald S UllersDepartment of Molecular Microbiology, Vrije Universiteit, 1081 HV, Amsterdam, The Netherlands.
Joen Luirink
Nellie Harms
Françoise Schwager
Costa Georgopoulos
Pierre Genevaux
Vrije Universiteit Amsterdam · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

It is known that the DnaK and Trigger Factor (TF) chaperones cooperate in the folding of newly synthesized cytosolic proteins in Escherichia coli. We recently showed that despite a very narrow temperature range of growth and high levels of aggregated cytosolic proteins, E. coli can tolerate deletion of both chaperones, suggesting that other chaperones might be involved in this process. Here, we show that the secretion-dedicated chaperone SecB efficiently suppresses both the temperature sensitivity and the aggregation-prone phenotypes of a strain lacking both TF and DnaK. SecB suppression is independent of a productive interaction with the SecA subunit of the translocon. Furthermore, in vitro cross-linking experiments demonstrate that SecB can interact both co- and posttranslationally with short nascent chains of both secretory and cytosolic proteins. Finally, we show that such cotranslational substrate recognition by SecB is greatly suppressed in the presence of ribosome-bound TF, but not by DnaK. Taken together, our data demonstrate that SecB acts as a bona fide generalized chaperone.

Indexed as

Bacterial ProteinsDNA-Directed RNA PolymerasesEscherichia coliEscherichia coli ProteinsHeat-Shock ProteinsHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsMolecular ChaperonesPeptidylprolyl IsomeraseProtein FoldingBacterial ProteinsDNA-Directed RNA PolymerasesdnaK protein, E coliEscherichia coli ProteinsHeat-Shock ProteinsHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsMolecular ChaperonesPeptidylprolyl IsomeraseRNA polymerase beta subunitSecB protein, Bacteriatrigger factor, E coli

Identifiers

PMID15128935
PMCPMC419649
OpenAlexW2025501168

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.