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Amyloid oligomers: diffuse oligomer-based transmission of yeast prions

Hideki Taguchi1, Shigeko Kawai-Noma

  • 1Department of Medical Genome Sciences, Graduate School of Frontier Sciences, University of Tokyo, Kashiwanoha, Kashiwa, Chiba, Japan. taguchi@k.u-tokyo.ac.jp

The FEBS Journal
|February 13, 2010
PubMed

Insights

Yeast prions, like the [PSI(+)] element involving the Sup35 protein, are infectious proteins. Their transmission relies on cytoplasmic prion protein oligomers, offering insights into prion propagation mechanisms.

Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • Prions are infectious proteins characterized by self-propagating amyloid conformations.
  • Budding yeast, Saccharomyces cerevisiae, serves as a model eukaryote for studying prion phenomena.
  • Yeast prions, such as [PSI(+)], are non-Mendelian, protein-based heritable elements.

Purpose of the Study:

  • To review the transmissible entities of yeast prions.
  • To focus on the mechanisms of prion propagation and transmission in yeast.
  • To highlight the role of the Sup35 protein in the [PSI(+)] prion.

Main Methods:

  • Review of existing genetic and dynamic studies of yeast prions.
  • Analysis of research on prion protein aggregation and transmission.
  • Focus on cytoplasmic prion protein species.

Main Results:

  • Oligomeric species of prion proteins dispersed in the cytoplasm are critical for transmission.
  • Dynamic aspects of prion proteins are key to understanding propagation mechanisms.
  • Non-Mendelian inheritance of yeast prions is mediated by protein aggregates.

Conclusions:

  • Yeast prions provide a tractable model for understanding prion biology.
  • Cytoplasmic prion protein oligomers are essential for prion transmission.
  • Further research into dynamic aspects of prion proteins can elucidate molecular mechanisms.

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