ArticleProceedings of the National Academy of Sciences of the United States of America2010
Ribosome-associated peroxiredoxins suppress oxidative stress-induced de novo formation of the [PSI+] prion in yeast.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 54 citations in OpenAlex.
- [SNG2], a prion form of Cut4/Apc1, confers non-Mendelian inheritance of heterochromatin silencing defect in fission yeast.Nucleic acids research · 2024Article
- Sequestrase chaperones protect against oxidative stress-induced protein aggregation and [PSI+] prion formation.PLoS genetics · 2024Article
- Methionine Sulfoxide Reductases Suppress the Formation of the [Antioxidants (Basel, Switzerland) · 2023Article
- Impact of Hydrogen Peroxide on Protein Synthesis in Yeast.Antioxidants (Basel, Switzerland) · 2021Review
- Cross-talk between redox signalling and protein aggregation.Biochemical Society transactions · 2020Review
- Causative Links between Protein Aggregation and Oxidative Stress: A Review.International journal of molecular sciences · 2019Review
- Endoplasmic reticulum (ER) stress-induced reactive oxygen species (ROS) are detrimental for the fitness of a thioredoxin reductase mutant.The Journal of biological chemistry · 2018Article
- Disrupting the cortical actin cytoskeleton points to two distinct mechanisms of yeast [PSI+] prion formation.PLoS genetics · 2017Article
- Site-specific mutagenesis of yeast 2-Cys peroxiredoxin improves heat or oxidative stress tolerance by enhancing its chaperone or peroxidase function.Protoplasma · 2017Article
- The copper transport-associated protein Ctr4 can form prion-like epigenetic determinants inMicrobial cell (Graz, Austria) · 2017Article
- Hydroxylation and translational adaptation to stress: some answers lie beyond the STOP codon.Cellular and molecular life sciences : CMLS · 2016Review
- Autophagy protects against de novo formation of the [PSI+] prion in yeast.Molecular biology of the cell · 2015Article
- Oxidative stress conditions increase the frequency of de novo formation of the yeast [PSI+] prion.Molecular microbiology · 2015Article
- Article
- Review
- One third of dynamic protein expression profiles can be predicted by a simple rate equation.Molecular bioSystems · 2014Article
- The yeast peroxiredoxin Tsa1 protects against protein-aggregate-induced oxidative stress.Journal of cell science · 2014Article
- Physiological and environmental control of yeast prions.FEMS microbiology reviews · 2014Review
- Loss of vacuolar H+-ATPase (V-ATPase) activity in yeast generates an iron deprivation signal that is moderated by induction of the peroxiredoxin TSA2.The Journal of biological chemistry · 2013Article
- Adaptive translation as a mechanism of stress response and adaptation.Annual review of genetics · 2013Review
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Peroxiredoxins (Prxs) are ubiquitous antioxidants that protect cells against oxidative stress. We show that the yeast Tsa1/Tsa2 Prxs colocalize to ribosomes and function to protect the Sup35 translation termination factor against oxidative stress-induced formation of its heritable [PSI(+)] prion conformation. In a tsa1 tsa2 [psi(-)] [PIN(+)] strain, the frequency of [PSI(+)] de novo formation is significantly elevated. The Tsa1/Tsa2 Prxs, like other 2-Cys Prxs, have dual activities as peroxidases and chaperones, and we show that the peroxidase activity is required to suppress spontaneous de novo [PSI(+)] prion formation. Molecular oxygen is required for [PSI(+)] prion formation as growth under anaerobic conditions prevents prion formation in the tsa1 tsa2 mutant. Conversely, oxidative stress conditions induced by exposure to hydrogen peroxide elevates the rate of de novo [PSI(+)] prion formation leading to increased suppression of all three termination codons in the tsa1 tsa2 mutant. Altered translational fidelity in [PSI(+)] strains may provide a mechanism that promotes genetic variation and phenotypic diversity (True HL, Lindquist SL (2000) Nature 407:477-483). In agreement, we find that prion formation provides yeast cells with an adaptive advantage under oxidative stress conditions, as elimination of the [PSI(+)] prion from tsa1 tsa2 mutants renders the resulting [psi(-)] [pin(-)] cells hypersensitive to hydrogen peroxide. These data support a model in which Prxs function to protect the ribosomal machinery against oxidative damage, but when these systems become overwhelmed, [PSI(+)] prion formation provides a mechanism for uncovering genetic traits that aid survival during oxidative stress conditions.
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