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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 Lindquist
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.

History

Publication status

  • Published

Journal

Science

ISSN

00368075

Issue

5483

Volume

289

Page range

1317-1321

Department affiliated with

  • Biochemistry Publications

Full text available

  • No

Peer reviewed?

  • Yes

Legacy Posted Date

2012-02-06

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