Evidence map›Paper›PMID 14726952›Full record

ArticleEMBO reports2004

In vivo analysis of the overlapping functions of DnaK and trigger factor.

Pierre Genevaux, France Keppel, Françoise Schwager, Petra S Langendijk-Genevaux, F Ulrich Hartl, Costa Georgopoulos

Abstract read
In one paragraph

Article in EMBO reports, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.

0numbers the graph read from it
0cells of the map it votes in
79citing 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

79 citing papers in PubMed.

  1. Article
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  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
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  11. Article
  12. Temperature Matters: Bacterial Response to Temperature Change.Journal of microbiology (Seoul, Korea) · 2023
    Review
  13. Frontiers in molecular biosciences · 2023
    Review
  14. The biogenesis of β-lactamase enzymes.Microbiology (Reading, England) · 2022
    Review
  15. Review
  16. Article
  17. Frontiers in microbiology · 2022
    Article
  18. Update on the Protein Homeostasis Network inFrontiers in microbiology · 2022
    Review
  19. Review
  20. Mechanisms of Cotranslational Protein Maturation in Bacteria.Frontiers in molecular biosciences · 2021
    Review

19 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

6 authors.

Pierre GenevauxDépartement de Biochimie Médicale, Centre Médical Universitaire, Genève, Switzerland. pierre.genevaux@medecine.unige.ch
France Keppel
Françoise Schwager
Petra S Langendijk-Genevaux
F Ulrich Hartl
Costa Georgopoulos

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Trigger factor (TF) is a ribosome-bound protein that combines catalysis of peptidyl-prolyl isomerization and chaperone-like activities in Escherichia coli. TF was shown to cooperate with the DnaK (Hsp70) chaperone machinery in the folding of newly synthesized proteins, and the double deletion of the corresponding genes (tig and dnaK) exhibited synthetic lethality. We used a detailed genetic approach to characterize various aspects of this functional cooperation in vivo. Surprisingly, we showed that under specific growth conditions, one can delete both dnaK and tig, indicating that bacterial survival can be maintained in the absence of these two major cytosolic chaperones. The strain lacking both DnaK and TF exhibits a very narrow temperature range of growth and a high level of aggregated proteins when compared to either of the single mutants. We found that, in the absence of DnaK, both the N-terminal ribosome-binding domain and the C-terminal domain of unknown function are essential for TF chaperone activity. In contrast, the central PPIase domain is dispensable. Taken together, our data indicate that under certain conditions, folding of newly synthesized proteins in E. coli is not totally dependent on an interaction with either TF and/or DnaK, and suggest that additional chaperones may be involved in this essential process.

Indexed as

Chaperonin 10Chaperonin 60Escherichia coli ProteinsGenetic Complementation TestHeat-Shock ProteinsHeat-Shock ResponseHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsMolecular ChaperonesPeptidylprolyl IsomerasePorinsProtein FoldingProtein Structure, TertiaryChaperonin 10Chaperonin 60dnaK protein, E coliEscherichia coli ProteinsHeat-Shock ProteinsHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsMolecular ChaperonesOmpF proteinPeptidylprolyl IsomerasePorinstrigger factor, E coli

Identifiers

PMID14726952
PMCPMC1298978

What OpenQuestion holds

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Registered trials

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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.