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- Title
Nucleated conformational conversion and the replication of conformational information by a prion determinant.
- Authors
Serio, T R; Cashikar, A G; Kowal, A S; Sawicki, G J; Moslehi, J J; Serpell, L; Arnsdorf, M F; Lindquist, S L
- Abstract
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.
- Publication
Science (New York, N.Y.), 2000, Vol 289, Issue 5483, p1317
- ISSN
0036-8075
- Publication type
Journal Article
- DOI
10.1126/science.289.5483.1317