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High-throughput Screening for Protein-based Inheritance in S. cerevisiae
08:12

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Published on: August 8, 2017

Prion stability.

Brian S Cox1, Lee J Byrne, Mick F Tuite

  • 1Department of Biosciences, University of Kent, Canterbury, Kent, UK.

Prion
|January 24, 2009
PubMed
Summary
This summary is machine-generated.

Yeast prion protein Sup35p transitions between psi(-) and psi(+) states. Factors influencing prion induction and reversion, including chaperones like Hsp104, are explored, alongside maintenance models.

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Protein Misfolding Cyclic Amplification of Prions
10:12

Protein Misfolding Cyclic Amplification of Prions

Published on: November 7, 2012

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Yeast Genetics

Background:

  • Prions are proteins that can adopt misfolded conformations, leading to disease.
  • In yeast, the Sup35p protein forms prions, influencing cellular phenotypes.
  • Understanding prion dynamics is crucial for comprehending protein-based inheritance.

Purpose of the Study:

  • To discuss factors affecting the spontaneous conversion of yeast prion states.
  • To explore conditions influencing the induction and reversion of prion forms.
  • To examine prion maintenance models and variants.

Main Methods:

  • Review of existing literature on yeast prion dynamics.
  • Analysis of factors influencing prion induction rates.
  • Discussion of chaperone activity (Hsp104) in prion reversion.
  • Examination of prion seed copy-number and partitioning.

Main Results:

  • Prion induction is influenced by non-prion protein levels, other prions, chaperone activity, and protein sequence.
  • Prion reversion is affected by Hsp104 activity, protein sequence, and other agents.
  • Prion variants and their phenotypic/genetic parameters are increasingly described.

Conclusions:

  • The conversion, induction, and reversion of yeast prions are complex processes influenced by multiple factors.
  • Chaperone activity, particularly Hsp104, plays a critical role in prion dynamics.
  • Maintenance models provide insights into the diverse nature of prion variants.