Journal
CELL
Volume 106, Issue 2, Pages 171-182Publisher
CELL PRESS
DOI: 10.1016/S0092-8674(01)00427-5
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Funding
- NIGMS NIH HHS [R01 GM056350, GM 56350] Funding Source: Medline
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Prions are self-propagating protein conformations. Recent research brought insight into prion propagation, but how they first appear is unknown. We previously established that the yeast non-Mendelian trait [PIN+] is required for the de novo appearance of the [PSI+] prion. Here, we show that the presence of prions formed by Rnq1 or Ure2 is sufficient to make cells [PIN+]. Thus, [PIN+] can be caused by more than one prion. Furthermore, an unbiased functional screen for [PIN+] prions uncovered the known prion gene, URE2, the proposed prion gene, NEW1, and nine novel candidate prion genes all carrying prion domains. Importantly, the de novo appearance of Rnq1::GFP prion aggregates also requires the presence of other prions, suggesting the existence of a general mechanism by which the appearance of prions is enhanced by heterologous prion aggregates.
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