ArticleThe Journal of biological chemistry2015
Hsp31 Is a Stress Response Chaperone That Intervenes in the Protein Misfolding Process.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 44 citations in OpenAlex.
- Control of heat and oxidative stress adaptation by the DJ-1 paralogs in Arabidopsis thaliana.Plant molecular biology · 2025Article
- Ubp2 modulates DJ-1-mediated redox-dependent mitochondrial dynamics in Saccharomyces cerevisiae.PLoS genetics · 2025Article
- Integrative Omics reveals changes in the cellular landscape of peroxisome-deficientMicrobial cell (Graz, Austria) · 2025Article
- The Reaction of the YeastInternational journal of molecular sciences · 2023Article
- Divergence in the Saccharomyces Species' Heat Shock Response Is Indicative of Their Thermal Tolerance.Genome biology and evolution · 2023Article
- Article
- A Yeast Chronological Lifespan Assay to Assess Activity of Proteasome Stimulators.Chembiochem : a European journal of chemical biology · 2021Article
- The Role of DJ-1 in Cellular Metabolism and Pathophysiological Implications for Parkinson's Disease.Cells · 2021Review
- Redox-dependent regulation of mitochondrial dynamics by DJ-1 paralogs in Saccharomyces cerevisiae.Redox biology · 2020Article
- Role of Alcohol Drinking in Alzheimer's Disease, Parkinson's Disease, and Amyotrophic Lateral Sclerosis.International journal of molecular sciences · 2020Review
- Saccharomyces cerevisiae Cytosolic Thioredoxins Control Glycolysis, Lipid Metabolism, and Protein Biosynthesis under Wine-Making Conditions.Applied and environmental microbiology · 2019Article
- Structural and functional insights into TRiC chaperonin from a psychrophilic yeast, Glaciozyma antarctica.Cell stress & chaperones · 2019Article
- Bifunctional Chloroplastic DJ-1B fromAntioxidants (Basel, Switzerland) · 2019Article
- Oxidative stress triggers aggregation of GFP-tagged Hsp31p, the budding yeast environmental stress response chaperone, and glyoxalase III.Cell stress & chaperones · 2018Article
- Randomized CRISPR-Cas Transcriptional Perturbation Screening Reveals Protective Genes against Alpha-Synuclein Toxicity.Molecular cell · 2017Article
- Methylglyoxal detoxification by a DJ-1 family protein provides dual abiotic and biotic stress tolerance in transgenic plants.Plant molecular biology · 2017Article
- Article
- The small heat shock protein Hsp31 cooperates with Hsp104 to modulate Sup35 prion aggregation.Prion · 2016Article
- Hsp31, a member of the DJ-1 superfamily, is a multitasking stress responder with chaperone activity.Prion · 2016Article
- Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
The Saccharomyces cerevisiae heat shock protein Hsp31 is a stress-inducible homodimeric protein that is involved in diauxic shift reprogramming and has glyoxalase activity. We show that substoichiometric concentrations of Hsp31 can abrogate aggregation of a broad array of substrates in vitro. Hsp31 also modulates the aggregation of α-synuclein (αSyn), a target of the chaperone activity of human DJ-1, an Hsp31 homolog. We demonstrate that Hsp31 is able to suppress the in vitro fibrillization or aggregation of αSyn, citrate synthase and insulin. Chaperone activity was also observed in vivo because constitutive overexpression of Hsp31 reduced the incidence of αSyn cytoplasmic foci, and yeast cells were rescued from αSyn-generated proteotoxicity upon Hsp31 overexpression. Moreover, we showed that Hsp31 protein levels are increased by H2O2, in the diauxic phase of normal growth conditions, and in cells under αSyn-mediated proteotoxic stress. We show that Hsp31 chaperone activity and not the methylglyoxalase activity or the autophagy pathway drives the protective effects. We also demonstrate reduced aggregation of the Sup35 prion domain, PrD-Sup35, as visualized by fluorescent protein fusions. In addition, Hsp31 acts on its substrates prior to the formation of large aggregates because Hsp31 does not mutually localize with prion aggregates, and it prevents the formation of detectable in vitro αSyn fibrils. These studies establish that the protective role of Hsp31 against cellular stress is achieved by chaperone activity that intervenes early in the protein misfolding process and is effective on a wide spectrum of substrate proteins, including αSyn and prion proteins.
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Registered trials
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.