Evidence map›Paper›PMID 29487911›Full record

ArticleScience advances2018

The force-dependent mechanism of DnaK-mediated mechanical folding.

Judit Perales-Calvo, David Giganti, Guillaume Stirnemann, Sergi Garcia-Manyes

Abstract read
In one paragraph

Article in Science advances, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Force-regulated chaperone activity of BiP/ERdj3 is opposite to their homologs DnaK/DnaJ.Protein science : a publication of the Protein Society · 2024
    Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. One-step asparaginyl endopeptidase (RSC chemical biology · 2022
    Article
  10. Active unfolding of the glucocorticoid receptor by the Hsp70/Hsp40 chaperone system in single-molecule mechanical experiments.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  11. Review
  12. Update on the Protein Homeostasis Network inFrontiers in microbiology · 2022
    Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
  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

4 authors.

Judit Perales-CalvoDepartment of Physics and Randall Division of Cell and Molecular Biophysics, King's College London, WC2R 2LS London, UK.ORCID 0000-0002-7897-2841
David GigantiDepartment of Physics and Randall Division of Cell and Molecular Biophysics, King's College London, WC2R 2LS London, UK.ORCID 0000-0001-5735-5679
Guillaume StirnemannCNRS Laboratoire de Biochimie Théorique, Institut de Biologie Physico-Chimique, Univ. Paris Denis Diderot, Sorbonne Paris Cité, PSL Research University, 13 rue Pierre et Marie Curie, 75005 Paris, France.ORCID 0000-0002-5631-5699
Sergi Garcia-ManyesDepartment of Physics and Randall Division of Cell and Molecular Biophysics, King's College London, WC2R 2LS London, UK.ORCID 0000-0001-5140-2606

Funding

Biotechnology and Biological Sciences Research Council BB/J00992X/1
6 · The paper itself

Abstract

It is well established that chaperones modulate the protein folding free-energy landscape. However, the molecular determinants underlying chaperone-mediated mechanical folding remain largely elusive, primarily because the force-extended unfolded conformation fundamentally differs from that characterized in biochemistry experiments. We use single-molecule force-clamp spectroscopy, combined with molecular dynamics simulations, to study the effect that the Hsp70 system has on the mechanical folding of three mechanically stiff model proteins. Our results demonstrate that, when working independently, DnaJ (Hsp40) and DnaK (Hsp70) work as holdases, blocking refolding by binding to distinct substrate conformations. Whereas DnaK binds to molten globule-like forms, DnaJ recognizes a cryptic sequence in the extended state in an unanticipated force-dependent manner. By contrast, the synergetic coupling of the Hsp70 system exhibits a marked foldase behavior. Our results offer unprecedented molecular and kinetic insights into the mechanisms by which mechanical force finely regulates chaperone binding, directly affecting protein elasticity.

Identifiers

PMID29487911
PMCPMC5817926

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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.