Conservation of Prion-Like Composition and Sequence in Prion-Formers and Prion-Like Proteins of Saccharomyces cerevisiae
Prions in eukaryotes have been linked to diseases, evolutionary capacitance, large-scale genetic control, and long-term memory formation. Prion formation and propagation have been studied extensively in the budding yeast Saccharomyces cerevisiae. Here, we have analysed the conservation of sequence and of prion-like composition for prion-forming proteins and for other prion-like proteins from S. cerevisiae, across three evolutionary levels. We discover that prion-like status is well-conserved for about half the set of prion-formers at the Saccharomycetes level, and that prion-forming domains evolve more quickly as sequences than other prion-like domains do. Such increased mutation rates may be linked to the acquisition of functional roles for prion-forming domains during the evolutionary epoch of Saccharomycetes. Domain scores for prion-like composition in S. cerevisiae are strongly correlated with scores for such composition weighted evolutionarily over the dozens of fungal species examined, indicating conservation of such prion-like status. Examples of notable prion-like proteins that are highly conserved both in sequence and prion-like composition are discussed.
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REFERENCES
- https://doi.org//10.1016/j.cell.2009.02.044
- https://doi.org//10.1186/s12862-016-0594-3
- https://doi.org//10.1186/s13062-016-0134-5
- https://doi.org//10.1093/nar/gkg095
- https://doi.org//10.1016/j.sbi.2011.02.005
- https://doi.org//10.1007/s00239-001-2309-6
- https://doi.org//10.1083/jcb.200807043
- https://doi.org//10.1080/19336896.2017.1356560
- https://doi.org//10.1073/pnas.1604478113
- https://doi.org//10.1016/j.celrep.2016.12.082
- https://doi.org//10.1128/EC.00015-13
- https://doi.org//10.1371/journal.pone.0026800
- https://doi.org//10.1186/1471-2164-14-316
- https://doi.org//10.1126/science.aao5654