Prion-inducing domain 2-114 of yeast Sup35 protein transforms in vitro into amyloid-like filaments
| Autor: | Roland Gebert, Peter Tittmann, Markus Aebi, Kurt Wüthrich, Heinz Gross, Chih-Yen King |
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| Rok vydání: | 1997 |
| Předmět: |
Fungal protein
Circular dichroism Amyloid Multidisciplinary Saccharomyces cerevisiae Proteins biology Prions Saccharomyces cerevisiae Ure2 macromolecular substances Biological Sciences biology.organism_classification Peptide Fragments Fungal prion Protein filament Fungal Proteins Biochemistry Biophysics Actin Peptide Termination Factors |
| Zdroj: | Proceedings of the National Academy of Sciences of the United States of America. 94(13) |
| ISSN: | 0027-8424 |
| Popis: | The yeast non-Mendelian genetic factor [PSI], which enhances the efficiency of tRNA-mediated nonsense suppression in Saccharomyces cerevisiae , is thought to be an abnormal cellular isoform of the Sup35 protein. Genetic studies have established that the N-terminal part of the Sup35 protein is sufficient for the genesis as well as the maintenance of [PSI]. Here we demonstrate that the N-terminal polypeptide fragment consisting of residues 2–114 of Sup35p, Sup35pN, spontaneously aggregates to form thin filaments in vitro . The filaments show a β-sheet-type circular dichroism spectrum, exhibit increased protease resistance, and show amyloid-like optical properties. It is further shown that filament growth in freshly prepared Sup35pN solutions can be induced by seeding with a dilute suspension of preformed filaments. These results suggest that the abnormal cellular isoform of Sup35p is an amyloid-like aggregate and further indicate that seeding might be responsible for the maintenance of the [PSI] element in vivo . |
| Databáze: | OpenAIRE |
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