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Conformational diversity in a yeast prion dictates its seeding specificity
1Department of Cellular and Molecular Pharmacology, University of California-San Francisco, 94143-0450, USA.
Nature
|March 10, 2001
Summary
Prion strains, like the yeast [PSI+] prion, arise from self-propagating conformational changes within proteins. These structural variations influence prion behavior and cross-species transmission barriers.
Area of Science:
- Molecular Biology
- Prion Biology
- Yeast Genetics
Background:
- Prions exhibit strain diversity, producing different phenotypes even in identical hosts.
- The molecular basis of prion strain diversity and interspecies transmission barriers is not fully understood.
Purpose of the Study:
- Investigate the role of conformational differences in prion strain diversity.
- Examine how these differences affect prion transmission.
Main Methods:
- Created a chimeric fusion protein from the prion domains of Saccharomyces cerevisiae and Candida albicans Sup35.
- Induced prion strains in vivo via transient overexpression.
- Propagated distinct amyloid conformations in vitro using seeded assays.
Main Results:
- The chimeric Sup35 formed alternate prion strains in vivo depending on the initiating Sup35 species.
- In vitro, the chimera propagated distinct amyloid conformations when seeded with different Sup35 fibers.
- Amyloid fiber conformations determined seeding specificity, showing species-dependent propagation.
Conclusions:
- Heritable prion strains result from self-propagating conformational differences within the prion protein.
- Conformational variations, along with primary protein structure, dictate a prion's species transmission barrier.
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