ArticleThe Journal of biological chemistry2003
Ure2, a prion precursor with homology to glutathione S-transferase, protects Saccharomyces cerevisiae cells from heavy metal ion and oxidant toxicity.
Article in The Journal of biological chemistry, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 70 citations in OpenAlex.
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- Transcriptional Profiling of theInternational journal of molecular sciences · 2022Article
- Increased Accumulation of Squalene in Engineered Yarrowia lipolytica through Deletion ofApplied and environmental microbiology · 2021Article
- Glutathione-coordinated metal complexes as substrates for cellular transporters.Metallomics : integrated biometal science · 2021Review
- Amelioration of Metal-Induced Cellular Stress by α-Lipoic Acid and Dihydrolipoic Acid through Antioxidative Effects in PC12 Cells and Caco-2 Cells.International journal of environmental research and public health · 2021Article
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- Engineering microbial phenotypes through rewiring of genetic networks.Nucleic acids research · 2017Article
- Transcriptomic responses of the basidiomycete yeast Sporobolomyces sp. to the mycotoxin patulin.BMC genomics · 2016Article
- Article
- Influence of specific HSP70 domains on fibril formation of the yeast prion protein Ure2.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2013Article
- The prion hypothesis: from biological anomaly to basic regulatory mechanism.Nature reviews. Molecular cell biology · 2010Review
- Ure2 is involved in nitrogen catabolite repression and salt tolerance via Ca2+ homeostasis and calcineurin activation in the yeast Hansenula polymorpha.The Journal of biological chemistry · 2010Article
- Perspectives for genetic engineering of poplars for enhanced phytoremediation abilities.Ecotoxicology (London, England) · 2010Review
- The fungal glutathione S-transferase system. Evidence of new classes in the wood-degrading basidiomycete Phanerochaete chrysosporium.Cellular and molecular life sciences : CMLS · 2009Review
- Novel glutaredoxin activity of the yeast prion protein Ure2 reveals a native-like dimer within fibrils.The Journal of biological chemistry · 2009Article
- Recent advances in nitrogen regulation: a comparison between Saccharomyces cerevisiae and filamentous fungi.Eukaryotic cell · 2008Review
- Moonlighting proteins in yeasts.Microbiology and molecular biology reviews : MMBR · 2008Review
- Stress-responsive Gln3 localization in Saccharomyces cerevisiae is separable from and can overwhelm nitrogen source regulation.The Journal of biological chemistry · 2007Article
- A peroxisomal glutathione transferase of Saccharomyces cerevisiae is functionally related to sulfur amino acid metabolism.Eukaryotic cell · 2006Article
- Yeast prions [URE3] and [PSI+] are diseases.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Ure2, the protein that negatively regulates GATA factor (Gln3, Gat1)-mediated transcription in Saccharomyces cerevisiae, possesses prion-like characteristics. Identification of metabolic and environmental factors that influence prion formation as well as any activities that prions or prion precursors may possess are important to understanding them and developing treatment strategies for the diseases in which they participate. Ure2 exhibits primary sequence and three-dimensional homologies to known glutathione S-transferases. However, multiple attempts over nearly 2 decades to demonstrate Ure2-mediated S-transferase activity have been unsuccessful, leading to the possibility that Ure2 may well not participate in glutathionation reactions. Here we show that Ure2 is required for detoxification of glutathione S-transferase substrates and cellular oxidants. ure2 Delta mutants are hypersensitive to cadmium and nickel ions and hydrogen peroxide. They are only slightly hypersensitive to diamide, which is nitrogen source-dependent, and minimally if at all hypersensitive to 1-chloro-2,4-dinitrobenzene, the most commonly used substrate for glutathione S-transferase enzyme assays. Therefore, Ure2 shares not only structural homology with various glutathione S-transferases, but ure2 mutations possess the same phenotypes as mutations in known S. cerevisiae and Schizosaccharomyces pombe glutathione S-transferase genes. These findings are consistent with Ure2 serving as a glutathione S-transferase in S. cerevisiae.
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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.