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Nucleated conformational conversion and the replication of conformational information by a prion determinant
journal contribution
posted on 2023-06-08, 07:50 authored by Tricia R Serio, Anil G Cashikar, Anthony S Kowal, George J Sawicki, Jahan J Moslehi, Louise SerpellLouise Serpell, Morton F Arnsdorf, Susan L LindquistPrion 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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Publication status
- Published
Journal
ScienceISSN
00368075External DOI
Issue
5483Volume
289Page range
1317-1321Department affiliated with
- Biochemistry Publications
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- No
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- Yes
Legacy Posted Date
2012-02-06Usage metrics
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