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Nucleated conformational conversion and the replication of conformational information by a prion determinant.
Serio, T R; Cashikar, A G; Kowal, A S; Sawicki, G J; Moslehi, J J; Serpell, L; Arnsdorf, M F; Lindquist, S L.
Afiliación
  • Serio TR; Department of Molecular Genetics and Cell Biology, Howard Hughes Medical Institute, University of Chicago, Chicago, IL 60637, USA.
Science ; 289(5483): 1317-21, 2000 Aug 25.
Article en En | MEDLINE | ID: mdl-10958771
Prion proteins can serve as genetic elements by adopting distinct physical and functional states that are self-perpetuating and heritable. The critical region of one prion protein, Sup35, is initially unstructured in solution and then forms self-seeded amyloid fibers. We examined in vitro the mechanism by which this state is attained and replicated. Structurally fluid oligomeric complexes appear to be crucial intermediates in de novo amyloid nucleus formation. Rapid assembly ensues when these complexes conformationally convert upon association with nuclei. This model for replicating protein-based genetic information, nucleated conformational conversion, may be applicable to other protein assembly processes.
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Priones / Proteínas Fúngicas / Proteínas de Saccharomyces cerevisiae / Amiloide Tipo de estudio: Prognostic_studies Idioma: En Revista: Science Año: 2000 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Priones / Proteínas Fúngicas / Proteínas de Saccharomyces cerevisiae / Amiloide Tipo de estudio: Prognostic_studies Idioma: En Revista: Science Año: 2000 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos