Evidence map›Paper›PMID 22809627›Full record

ArticleMolecular biology of the cell2012

The yeast Hsp70 Ssa1 is a sensor for activation of the heat shock response by thiol-reactive compounds.

Yanyu Wang, Patrick A Gibney, James D West, Kevin A Morano

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed, 1 pooled it
3.1field-weighted citation impact, top 8% 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

43 citing papers in PubMed, 1 synthesis or guideline pooled it, 71 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Role of spt23 in Saccharomyces cerevisiae thermal tolerance.Applied microbiology and biotechnology · 2022
    Article
  12. Review
  13. Review
  14. Article
  15. Impact of Hydrogen Peroxide on Protein Synthesis in Yeast.Antioxidants (Basel, Switzerland) · 2021
    Review
  16. Review
  17. Article
  18. The Journal of biological chemistry · 2020
    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 at 3 institutions in 1 country.

Yanyu WangDepartment of Microbiology and Molecular Genetics, University of Texas Medical School at Houston, Houston, TX 77030, USA.
Patrick A Gibney
James D West
Kevin A Morano
The University of Texas at Austin · USCollege of Wooster · USThe University of Texas Health Science Center at Houston · US

Funding

Hsp110 protein chaperone function in yeastR01GM074696 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI MORANO, KEVIN ANTHONY · 2006 to 2015
$2.8M
NIGMS NIH HHS GM074696NIGMS NIH HHS R01 GM074696
6 · The paper itself

Abstract

The heat shock transcription factor HSF1 governs the response to heat shock, oxidative stresses, and xenobiotics through unknown mechanisms. We demonstrate that diverse thiol-reactive molecules potently activate budding yeast Hsf1. Hsf1 activation by thiol-reactive compounds is not consistent with the stresses of misfolding of cytoplasmic proteins or cytotoxicity. Instead, we demonstrate that the Hsp70 chaperone Ssa1, which represses Hsf1 in the absence of stress, is hypersensitive to modification by a thiol-reactive probe. Strikingly, mutation of two conserved cysteine residues to serine in Ssa1 rendered cells insensitive to Hsf1 activation and subsequently induced thermotolerance by thiol-reactive compounds, but not by heat shock. Conversely, substitution with the sulfinic acid mimic aspartic acid resulted in constitutive Hsf1 activation. Cysteine 303, located within the nucleotide-binding domain, was found to be modified in vivo by a model organic electrophile, demonstrating that Ssa1 is a direct target for thiol-reactive molecules through adduct formation. These findings demonstrate that Hsp70 is a proximal sensor for Hsf1-mediated cytoprotection and can discriminate between two distinct environmental stressors.

Indexed as

Heat-Shock ResponseAdenosine TriphosphatasesAspartic AcidBinding SitesDiamideDithiothreitolDNA-Binding ProteinsHeat-Shock ProteinsHSP70 Heat-Shock ProteinsHydrogen PeroxideMaleatesOxidative StressPentacyclic TriterpenesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSulfhydryl CompoundsAdenosine TriphosphatasesAspartic AcidcelastrolDiamidediethyl maleateDithiothreitolDNA-Binding ProteinsHeat-Shock ProteinsHSF1 protein, S cerevisiaeHSP70 Heat-Shock ProteinsHydrogen PeroxideMaleatesPentacyclic TriterpenesSaccharomyces cerevisiae ProteinsSSA1 protein, S cerevisiaeSulfhydryl CompoundsTranscription FactorsTriterpenes

Identifiers

PMID22809627
PMCPMC3469052
OpenAlexW2090745019

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.