ArticleGenetics2014
Sporadic distribution of prion-forming ability of Sup35p from yeasts and fungi.
Article in Genetics, 2014. 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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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
21 citing papers in PubMed.
- Article
- p53 amyloid pathology is correlated with higher cancer grade irrespective of the mutant or wild-type form.Journal of cell science · 2023Article
- Review
- Melatonin: Regulation of Prion Protein Phase Separation in Cancer Multidrug Resistance.Molecules (Basel, Switzerland) · 2022Review
- Review
- Prion-like low-complexity sequences: Key regulators of protein solubility and phase behavior.The Journal of biological chemistry · 2019Review
- Review
- Anti-Prion Systems in Yeast and Inositol Polyphosphates.Biochemistry · 2018Article
- [PSI+] prion propagation is controlled by inositol polyphosphates.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Evidence of a Prion-Like Transmission of p53 Amyloid in Saccharomyces cerevisiae.Molecular and cellular biology · 2017Article
- Epigenetic inheritance, prions and evolution.Journal of genetics · 2017Review
- Hsp104 disaggregase at normal levels cures many [Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- The copper transport-associated protein Ctr4 can form prion-like epigenetic determinants inMicrobial cell (Graz, Austria) · 2017Article
- Yeast and Fungal Prions.Cold Spring Harbor perspectives in biology · 2016Review
- Functional Translational Readthrough: A Systems Biology Perspective.PLoS genetics · 2016Review
- Prions are affected by evolution at two levels.Cellular and molecular life sciences : CMLS · 2016Review
- Emergence and evolution of yeast prion and prion-like proteins.BMC evolutionary biology · 2016Article
- Yeast and Fungal Prions: Amyloid-Handling Systems, Amyloid Structure, and Prion Biology.Advances in genetics · 2016Article
- Nonsense codon suppression in fission yeast due to mutations of tRNA(Ser.11) and translation release factor Sup35 (eRF3).Current genetics · 2015Article
- Yeast prions: structure, biology, and prion-handling systems.Microbiology and molecular biology reviews : MMBR · 2015Review
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Sup35p of Saccharomyces cerevisiae can form the [PSI+] prion, an infectious amyloid in which the protein is largely inactive. The part of Sup35p that forms the amyloid is the region normally involved in control of mRNA turnover. The formation of [PSI+] by Sup35p's from other yeasts has been interpreted to imply that the prion-forming ability of Sup35p is conserved in evolution, and thus of survival/fitness/evolutionary value to these organisms. We surveyed a larger number of yeast and fungal species by the same criteria as used previously and find that the Sup35p from many species cannot form prions. [PSI+] could be formed by the Sup35p from Candida albicans, Candida maltosa, Debaromyces hansenii, and Kluyveromyces lactis, but orders of magnitude less often than the S. cerevisiae Sup35p converts to the prion form. The Sup35s from Schizosaccharomyces pombe and Ashbya gossypii clearly do not form [PSI+]. We were also unable to detect [PSI+] formation by the Sup35ps from Aspergillus nidulans, Aspergillus fumigatus, Magnaporthe grisea, Ustilago maydis, or Cryptococcus neoformans. Each of two C. albicans SUP35 alleles can form [PSI+], but transmission from one to the other is partially blocked. These results suggest that the prion-forming ability of Sup35p is not a conserved trait, but is an occasional deleterious side effect of a protein domain conserved for another function.
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