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A more recent version of this article appeared on August 8, 2003
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M303000200v1
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Papers In Press, published online ahead of print May 30, 2003
J. Biol. Chem, 10.1074/jbc.M303000200
Submitted on March 24, 2003
Revised on May 19, 2003
Accepted on May 30, 2003

Assembly of the yeast prion Ure2p into protein fibrils: Thermodynamic and kinetic characterization

Nicolas Fay, Yuji Inoue, Luc Bousset, Hideki Taguchi, and Ronald Melki

Laboratoire d'Enzymologie et Biochimie Structurales, CNRS, 91198, Gif-sur-Yvette Cedex

Corresponding Author: melki{at}lebs.cnrs-gif.fr

The [URE3] phenotype in Saccharomyces cerevisiae propagates by a prion mechanism, involving the aggregation of the normally soluble and highly helical protein Ure2. Previous data have shown that the protein spontaneously forms in vitro long, straight, insoluble fibrils at neutral pH that are similar to amyloids in that they bind Congo red and show green-yellow birefringence and have an increased resistance to proteolysis. These fibrils are not amyloids as they are are devoid of a cross-beta core. Here we further document the mechanism of assembly of Ure2p into fibrils. The critical concentration for Ure2p assembly is measured and the minimal size of the nuclei that are the precursors of Ure2p fibrils determined. Our data indicate that the assembly process is irreversible with as a consequence a very low critical concentration. By analyzing the elongation rates of preformed fibrils and combining the results with single-fiber imaging experiments of a variant Ure2p labeled by fluorescent dyes, we reveal the polarity of the fibrils and differences in the elongation rates at their ends. These results bring novel insight in the process of Ure2p assembly into fibrils and the mechanism of propagation of yeast prions.


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