ArticleJournal of cell science2014
The yeast peroxiredoxin Tsa1 protects against protein-aggregate-induced oxidative stress.
Article in Journal of cell science, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 78 citations in OpenAlex.
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- The interactome of the Bakers' yeast peroxiredoxin Tsa1 implicates it in redox regulation of intermediary metabolism, glycolysis, and zinc homeostasis.Metallomics : integrated biometal science · 2025Article
- Identification ofAntioxidants (Basel, Switzerland) · 2025Article
- Direct binding of arsenicals to nuclear transport factors disrupts nucleocytoplasmic transport.bioRxiv : the preprint server for biology · 2025Article
- The mitochondrial quality control system: a new target for exercise therapeutic intervention in the treatment of brain insulin resistance-induced neurodegeneration in obesity.International journal of obesity (2005) · 2024Review
- Sequestrase chaperones protect against oxidative stress-induced protein aggregation and [PSI+] prion formation.PLoS genetics · 2024Article
- Common virulence factors betweenCurrent research in microbial sciences · 2024Review
- Formation of Transient Protein Aggregate-like Centers Is a General Strategy Postponing Degradation of Misfolded Intermediates.International journal of molecular sciences · 2023Article
- The Metabolism of Reactive Oxygen Species and Their Effects on Lipid Biosynthesis of Microalgae.International journal of molecular sciences · 2023Review
- Article
- Peroxisomal support of mitochondrial respiratory efficiency promotes ER stress survival.Journal of cell science · 2022Article
- Protein Aggregation in the Pathogenesis of Ischemic Stroke.Cellular and molecular neurobiology · 2021Review
- A comparative proteomic analysis of Candida species in response to the oxidizing agent cumene hydroperoxide.Archives of microbiology · 2021Article
- Repositioning antispasmodic drug Papaverine for the treatment of chronic myeloid leukemia.Pharmacological reports : PR · 2021Article
- Adaptability of the ubiquitin-proteasome system to proteolytic and folding stressors.The Journal of cell biology · 2021Article
- Microorganisms: A Potential Source of Bioactive Molecules for Antioxidant Applications.Molecules (Basel, Switzerland) · 2021Review
- Inhibition of mTOR decreases insoluble proteins burden by reducing translation in C. elegans.Biogerontology · 2021Article
- A curious case of cysteines in human peroxiredoxin I.Redox biology · 2020Article
- Cross-talk between redox signalling and protein aggregation.Biochemical Society transactions · 2020Review
- Exploring the bi-directional relationship between autophagy and Alzheimer's disease.CNS neuroscience & therapeutics · 2020Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Peroxiredoxins are ubiquitous thiol-specific proteins that have multiple functions in stress protection, including protection against oxidative stress. Tsa1 is the major yeast peroxiredoxin and we show that it functions as a specific antioxidant to protect the cell against the oxidative stress caused by nascent-protein misfolding and aggregation. Yeast mutants lacking TSA1 are sensitive to misfolding caused by exposure to the proline analogue azetidine-2-carboxylic acid (AZC). AZC promotes protein aggregation, and its toxicity to a tsa1 mutant is caused by the production of reactive oxygen species (ROS). The generation of [rho(0)] cells, which lack mitochondrial DNA, rescues the tsa1 mutant AZC sensitivity, indicating that mitochondria are the source of ROS. Inhibition of nascent-protein synthesis with cycloheximide prevents AZC-induced protein aggregation and abrogates ROS generation, confirming that the formation of aggregates causes ROS production. Protein aggregation is accompanied by mitochondrial fragmentation, and we show that Tsa1 localises to the sites of protein aggregation. Protein aggregates are formed adjacent to mitochondria, and our data indicate that active mitochondria generate ROS. These data indicate a new role for peroxiredoxins in protecting against ROS that are generated as a result of protein misfolding and aggregate formation.
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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.