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

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Strain-specific sequences required for yeast [PSI+] prion propagation.

Hsiang-Yu Chang¹, Jia-Yu Lin, Han-Chung Lee

¹Institute of Molecular Biology, Academia Sinica, Taipei 11529, Taiwan.

Proceedings of the National Academy of Sciences of the United States of America

|September 2, 2008

Summary

Yeast prion strains ([VH], [VK], [VL]) are distinct Sup35 protein folding patterns. Specific Sup35 protein sequences dictate the in vivo propagation of each prion strain, revealing key regions for amyloid conformation.

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Area of Science:

Biochemistry
Molecular Biology
Structural Biology

Background:

Prion strains arise from protein polymorphism, where a single polypeptide adopts various self-propagating cross-beta structures.
The yeast prion [PSI] involves amyloid conformers of the Sup35 protein, a translation termination factor.
Three characterized yeast prion strains are [VH], [VK], and [VL].

Purpose of the Study:

To identify specific Sup35 protein sequences essential for the in vivo propagation of the [VH], [VK], and [VL] yeast prion strains.
To define minimal polypeptide segments encoding prion conformations through in vitro assembly and infectivity assays.

Main Methods:

Introducing mutations (proline substitutions, glycine insertions) in the N-terminal 5-55 residues of Sup35.
Assaying prion strain propagation in yeast following mutagenesis.
Assembling recombinant Sup35 fragments on purified prion nuclei to form amyloid fibers in vitro.
Assaying the infectivity of in vitro assembled amyloid fibers in yeast.

Main Results:

Mutations selectively interfered with the propagation of specific prion strains: [VH] requires residues 7-21, [VK] requires residues 9-37, and [VL] requires residues 5-52.
In vitro studies defined minimal polypeptide segments encoding prion conformations.
For [VK] and [VL], minimal fragments matched mutation-defined sequences; for [VH], a longer fragment (Sup 1-53) was necessary.

Conclusions:

Specific N-terminal sequences of Sup35 are critical for the in vivo propagation of distinct prion strains.
Amyloid polymorphism in other proteins may similarly involve varied polypeptide stretches forming distinct cross-beta amyloid cores.