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Nucleated Conformational Conversion and the Replication of Conformational Information by a Prion Determinant
Tricia R. Serio, Anil G. Cashikar, Anthony S. Kowal, George J. Sawicki, Jahan J. Moslehi, Louise Serpell, Morton F. Arnsdorf and Susan L. Lindquist
New Series, Vol. 289, No. 5483 (Aug. 25, 2000), pp. 1317-1321
Published by: American Association for the Advancement of Science
Stable URL: http://www.jstor.org/stable/3077621
Page Count: 5
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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.
Science © 2000 American Association for the Advancement of Science