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Suicidal [PSI+] is a lethal yeast prion.

Ryan P McGlinchey1, Dmitry Kryndushkin, Reed B Wickner

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This summary is machine-generated.

Many yeast prion variants, including [PSI(+)] and [URE3], cause severe growth defects or lethality. This challenges the notion that yeast prions are generally benign, revealing a more realistic impact of prion phenomena.

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Area of Science:

  • Molecular biology
  • Yeast genetics
  • Prion biology

Background:

  • The yeast prion [PSI(+)] is a self-templating form of the essential translation termination factor Sup35p.
  • Mild [PSI(+)] variants are often studied and do not impair yeast growth, suggesting potential protective roles.
  • Other yeast prions, like [URE3] (a prion of Ure2p), are also studied for their biological roles.

Purpose of the Study:

  • To investigate the fitness consequences of diverse [PSI(+)] and [URE3] prion variants in yeast.
  • To determine the prevalence and impact of "sick" or "lethal" prion variants.
  • To provide a more comprehensive understanding of prion behavior beyond commonly studied mild variants.

Main Methods:

  • Generation and characterization of various [PSI(+)] and [URE3] prion variants in Saccharomyces cerevisiae.
  • Growth assays to assess the fitness and viability of yeast strains harboring different prion variants.
  • Genetic analysis to identify conditions or genetic modifications that affect prion-induced phenotypes.

Main Results:

  • Over 50% of [PSI(+)] variants analyzed were found to be detrimental, causing sickness or lethality.
  • "Killer [PSI(+)]" variants only supported growth when a truncated form of Sup35p (Sup35C) was co-expressed.
  • These detrimental [PSI(+)] variants were rapidly selected against, leading to loss of the prion or selection of non-detrimental variants.
  • Certain [URE3] prion variants also exhibited slower growth compared to cells lacking the Ure2p prion domain (ure2Δ).

Conclusions:

  • The study reveals that many yeast prion variants, contrary to previous assumptions, impose significant fitness costs.
  • The existence of "killer" prions necessitates a more nuanced view of prion biology and their impact on host cell physiology.
  • Focusing solely on mild prion variants provides an incomplete picture; a broader analysis including detrimental variants is crucial for understanding prion phenomena.