NR AKSD
AU Serio,T.R.; Cashikar,A.G.; Kowal,A.S.; Sawicki,G.J.; Moslehi,J.J.; Serpell,L.; Arnsdorf,M.F.; Lindquist,S.L.
TI Nucleated conformational conversion and the replication of conformational information by a prion determinant
QU Science 2000 Aug 25; 289(5483): 1317-21
PT journal article
AB 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.
MH Amyloid/*chemistry; Biopolymers/chemistry; Centrifugation, Density Gradient; Circular Dichroism; Electrophoresis, Polyacrylamide Gel; Endopeptidases/metabolism; Fungal Proteins/*chemistry/metabolism/ultrastructure; Kinetics; Light; Micelles; Microscopy, Atomic Force; Microscopy, Electron; Models, Chemical; Prions/*chemistry/metabolism/ultrastructure; Protein Conformation; Protein Folding; Scattering, Radiation; Solubility; Sonication; Support, Non-U.S. Gov't; Support, U.S. Gov't, Non-P.H.S.; Support, U.S. Gov't, P.H.S.
AD Department of Molecular Genetics and Cell Biology, Howard Hughes Medical Institute, University of Chicago, Chicago, IL 60637, USA
SP englisch
PO USA
EA pdf-Datei und HTML-Version