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Peptide sequences converting polyglutamine into a prion in yeast.

Wataru Odani1, Kazuhiro Urata, Momoko Okuda

  • 1Department of Medical Genome Sciences, Graduate School of Frontier Sciences, The University of Tokyo, Kashiwa, Chiba, Japan.

The FEBS Journal
|November 20, 2014
PubMed
Summary

Amyloid protein aggregates can be transmissible, blurring lines between neurodegenerative diseases. Researchers found specific peptides can convert non-transmissible polyglutamine (polyQ) amyloids into transmissible forms in yeast.

Keywords:
Sup35amyloidsfluorescence correlation spectroscopypolyglutamineyeast prions

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Area of Science:

  • Protein aggregation and prion biology.
  • Molecular mechanisms of protein misfolding and transmission.
  • Yeast as a model organism for studying amyloid dynamics.

Background:

  • Amyloids are ordered protein aggregates with cross-β sheet structures.
  • Prions are infectious amyloids causing transmissible spongiform encephalopathies.
  • The distinction between transmissible and non-transmissible amyloids, like those in Alzheimer's disease, is becoming less clear.

Purpose of the Study:

  • To investigate the dynamics and properties of polyglutamine (polyQ) amyloids in yeast.
  • To understand the mechanism distinguishing transmissible from non-transmissible amyloids.
  • To identify factors that can convert non-transmissible amyloids into transmissible forms.

Main Methods:

  • Utilized yeast cells to study polyglutamine (polyQ) amyloid formation and transmission.
  • Compared the aggregation propensity of polyQ with the yeast prion Sup35.
  • Screened peptides that could convert non-transmissible polyQ aggregates into transmissible ones.
  • Investigated the cellular dynamics of these modified polyQ aggregates.

Main Results:

  • Polyglutamine (polyQ) exhibited a higher tendency to form aggregates than the yeast prion Sup35.
  • Identified specific peptides that, when flanking the polyQ stretch, converted non-transmissible polyQ aggregates into transmissible forms.
  • Observed distinct cellular dynamics associated with the conversion process.

Conclusions:

  • The boundary between transmissible and non-transmissible amyloids is not absolute.
  • Specific molecular interactions, such as flanking peptides, can alter amyloid transmissibility.
  • Yeast models provide a valuable platform for dissecting the mechanisms of amyloid transmission.