Self-Seeded Fibers Formed by Sup35, the Protein Determinant of [ PSI+], a Heritable Prion-like Factor of S. cerevisiae

The [ PSI +] factor of S. cerevisiae represents a new form of inheritance: cytosolic transmission of an altered phenotype is apparently based upon inheritance of an altered protein structure rather than an altered nucleic acid. The molecular basis of its propagation is unknown. We report that purifi...

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Bibliographic Details
Published in:Cell 1997-05, Vol.89 (5), p.811-819
Main Authors: Glover, John R, Kowal, Anthony S, Schirmer, Eric C, Patino, Maria M, Liu, Jia-Jia, Lindquist, Susan
Format: Article
Language:English
Subjects:
Fungal Proteins - chemistry
Fungal Proteins - ultrastructure
Humans
Microscopy, Electron
Peptide Termination Factors
Prions - chemistry
Prions - ultrastructure
Protein Conformation
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins
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Summary:The [ PSI +] factor of S. cerevisiae represents a new form of inheritance: cytosolic transmission of an altered phenotype is apparently based upon inheritance of an altered protein structure rather than an altered nucleic acid. The molecular basis of its propagation is unknown. We report that purified Sup35 and subdomains that induce [ PSI +] elements in vivo form highly ordered fibers in vitro. Fibers bind Congo red and are rich in β sheet, characteristics of amyloids found in certain human diseases, including the prion diseases. Some fibers have distinct structures and these, once initiated, are self-perpetuating. Preformed fibers greatly accelerate fiber formation by unpolymerized protein. These data support a “protein-only” seeded polymerization model for the inheritance of [ PSI +].
ISSN:0092-8674
1097-4172
DOI:10.1016/S0092-8674(00)80264-0