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An efficient protein transformation protocol for introducing prions into yeast.

Motomasa Tanaka1, Jonathan S Weissman

  • 1Department of Cellular and Molecular Pharmacology, Howard Hughes Medical Institute, University of California San Francisco, 94143, USA.

Methods in Enzymology
|October 19, 2006
PubMed
Summary

Researchers developed a new protein transformation method for yeast, enabling efficient introduction of prion particles. This technique allows for de novo induction of yeast prion states and the creation of distinct prion strains from different protein conformations.

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Yeast Genetics

Background:

  • Introducing proteins into cells is challenging compared to nucleic acid transformation.
  • Yeast prion states, like [PSI(+)], are protein-based and heritable.
  • Understanding prion structure and propagation is crucial for studying protein misfolding diseases.

Purpose of the Study:

  • To develop a facile and efficient protein transformation protocol for yeast.
  • To investigate the de novo induction of yeast prion states using in vitro or in vivo produced prion particles.
  • To explore the generation and characterization of distinct prion strains based on protein conformation.

Main Methods:

  • Developed a protein transformation protocol for introducing prion particles into yeast.

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  • Used in vitro-produced or purified in vivo prion particles composed of Sup35p fragments.
  • Generated distinct amyloid conformations of the Sup35p fragment Sup-NM.
  • Infected yeast with different Sup-NM amyloid conformations to observe prion strain formation.

    • Main Results:

    • The protein transformation protocol achieved high efficiencies (approaching 100%) for de novo induction of the [PSI(+)] prion state.
    • Distinct Sup-NM amyloid conformations generated distinct [PSI(+)] prion strains.
    • Heritable differences in prion strains directly correlate with self-propagating differences in protein conformations.

    Conclusions:

    • The developed protein transformation protocol is effective for yeast prion studies.
    • Prion strain diversity arises directly from distinct, self-propagating protein conformations.
    • This method bridges in vitro and in vivo studies, facilitating research into prion inheritance and protein structure-function relationships.