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Mapping of Prion Structures in the Yeast Rnq1.

Arthur A Galliamov1, Alena D Malukhina1,2, Vitaly V Kushnirov1

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|March 28, 2024
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This study reveals that the prion structures of the yeast Rnq1 protein differ from previous predictions and that Rnq1-GFP fusions are unreliable for studying its prion properties. These findings impact yeast prion research.

Keywords:
amyloidmass spectrometryprionprion structure mappingproteinase Kyeast

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Yeast Genetics

Background:

  • The Rnq1 protein is a well-characterized yeast prion with a large, potentially prionogenic C-terminal region.
  • Previous research suggested only the C-terminal 40 residues form the prion structure, but this is re-evaluated here.

Purpose of the Study:

  • To map the actual and potential prion structures of Rnq1 and its C-terminal variants.
  • To investigate the reliability of Rnq1-GFP fusions for studying prion properties.

Main Methods:

  • Partial proteinase K digestion was used to analyze Rnq1 and its truncated variants in [RNQ+] yeast strains.
  • Microscopic observation of aggregation patterns for Rnq1 hybrid proteins.

Main Results:

  • Actual Rnq1 prion structures often differed from computational predictions and previous studies.
  • Aggregation patterns of Rnq1 hybrids varied significantly from Sup35 prion aggregates.
  • GFP fusion at the Rnq1 C-terminus inhibited prion formation, questioning its use in prior research.

Conclusions:

  • The C-terminal region of Rnq1 involved in prion formation is more complex than previously thought.
  • Rnq1-GFP fusions are not suitable for accurately studying Rnq1 prion characteristics.
  • Findings necessitate a re-evaluation of existing yeast prion research methodologies.