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J. Biol. Chem., Vol. 279, Issue 49, 50962-50968, December 3, 2004

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The [URE3] Yeast Prion Results from Protein Aggregates That Differ from Amyloid Filaments Formed in Vitro^*

Leslie Ripaud, Laurent Maillet, Françoise Immel-Torterotot, Fabien Durand, and Christophe Cullin

From the Institut de Biochimie et Génétique Cellulaires, 1, rue Camille Saint Saëns, UMR 5095, CNRSI Université Bordeaux 2 Victor Segalen, 33077 Bordeaux cedex France

The [URE3] yeast prion is a self-propagating inactive form of the Ure2 protein. Ure2p is composed of two domains, residues 1–93, the prion-forming domain, and the remaining C-terminal part of the protein, which forms the functional domain involved in nitrogen catabolite repression. In vitro, Ure2p forms amyloid filaments that have been proposed to be the aggregated prion form found in vivo. Here we showed that the biochemical characteristics of these two species differ. Protease digestions of Ure2p filaments and soluble Ure2p are comparable when analyzed by Coomassie staining as by Western blot. However, this finding does not explain the pattern specifically observed in [URE3] strains. Antibodies raised against the C-terminal part of Ure2p revealed the existence of proteolysis sites efficiently cleaved when [URE3], but not wild-type crude extracts, were submitted to limited proteolysis. The same antibodies lead to an equivalent digestion pattern when recombinant Ure2p (either soluble or amyloid) was analyzed in the same way. These results strongly suggest that aggregated Ure2p in [URE3] yeast cells is different from the amyloid filaments generated in vitro.

Received for publication, August 2, 2004 , and in revised form, September 16, 2004.

^* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Supported by a BDI "CNRS-Région Aquitaine" fellowship.

To whom correspondence should be addressed. Tel.: 33-556-999-017; Fax: 33-556-999-017; E-mail: Christophe.Cullin{at}ibgc.u-bordeaux2.fr.

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				F. Immel, Y. Jiang, Y.-Q. Wang, C. Marchal, L. Maillet, S. Perrett, and C. Cullin In Vitro Analysis of SpUre2p, a Prion-related Protein, Exemplifies the Relationship between Amyloid and Prion J. Biol. Chem., March 16, 2007; 282(11): 7912 - 7920. [Abstract] [Full Text] [PDF]