ArticleThe Journal of biological chemistry2011
Methionine oxidation of Sup35 protein induces formation of the [PSI+] prion in a yeast peroxiredoxin mutant.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 35 citations in OpenAlex.
- Mechanisms and regulation of substrate degradation by the 26S proteasome.Nature reviews. Molecular cell biology · 2025Review
- 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
- Increased levels of mitochondrial import factor Mia40 prevent the aggregation of polyQ proteins in the cytosol.The EMBO journal · 2021Article
- Review
- Article
- Endonucleolytic cleavage in the expansion segment 7 of 25S rRNA is an early marker of low-level oxidative stress in yeast.The Journal of biological chemistry · 2017Article
- Epigenetic inheritance, prions and evolution.Journal of genetics · 2017Review
- Disrupting the cortical actin cytoskeleton points to two distinct mechanisms of yeast [PSI+] prion formation.PLoS genetics · 2017Article
- The copper transport-associated protein Ctr4 can form prion-like epigenetic determinants inMicrobial cell (Graz, Austria) · 2017Article
- Methionine sulfoxide reductase A affects β-amyloid solubility and mitochondrial function in a mouse model of Alzheimer's disease.American journal of physiology. Endocrinology and metabolism · 2016Article
- 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
- Review
- Article
- Physiological and environmental control of yeast prions.FEMS microbiology reviews · 2014Review
- Methionine oxidation perturbs the structural core of the prion protein and suggests a generic misfolding pathway.The Journal of biological chemistry · 2012Article
- Prions in yeast.Genetics · 2012Review
- Impact of methionine oxidation as an initial event on the pathway of human prion protein conversion.PrionArticle
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The frequency with which the yeast [PSI(+)] prion form of Sup35 arises de novo is controlled by a number of genetic and environmental factors. We have previously shown that in cells lacking the antioxidant peroxiredoxin proteins Tsa1 and Tsa2, the frequency of de novo formation of [PSI(+)] is greatly elevated. We show here that Tsa1/Tsa2 also function to suppress the formation of the [PIN(+)] prion form of Rnq1. However, although oxidative stress increases the de novo formation of both [PIN(+)] and [PSI(+)], it does not overcome the requirement of cells being [PIN(+)] to form the [PSI(+)] prion. We use an anti-methionine sulfoxide antibody to show that methionine oxidation is elevated in Sup35 during oxidative stress conditions. Abrogating Sup35 methionine oxidation by overexpressing methionine sulfoxide reductase (MSRA) prevents [PSI(+)] formation, indicating that Sup35 oxidation may underlie the switch from a soluble to an aggregated form of Sup35. In contrast, we were unable to detect methionine oxidation of Rnq1, and MSRA overexpression did not affect [PIN(+)] formation in a tsa1 tsa2 mutant. The molecular basis of how yeast and mammalian prions form infectious amyloid-like structures de novo is poorly understood. Our data suggest a causal link between Sup35 protein oxidation and de novo [PSI(+)] prion formation.
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