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J. Biol. Chem., Vol. 282, Issue 11, 7912-7920, March 16, 2007

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In Vitro Analysis of SpUre2p, a Prion-related Protein, Exemplifies the Relationship between Amyloid and Prion^*

Francoise Immel¹, Yi Jiang¹, Yi-Qian Wang^¶, Christelle Marchal, Laurent Maillet, Sarah Perrett², and Christophe Cullin³

From the IBGC, UMR5095 CNRS-Université Bordeaux2, 1, rue Camille Saint Saens, 33077 Bordeaux cedex, France, the National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang District, Beijing 100101, China, and the ^¶Graduate School of the Chinese Academy of Sciences, Beijing 100039, China

The yeast Saccharomyces cerevisiae contains in its proteome at least three prion proteins. These proteins (Ure2p, Sup35p, and Rnq1p) share a set of remarkable properties. In vivo, they form aggregates that self-perpetuate their aggregation. This aggregation is controlled by Hsp104, which plays a major role in the growth and severing of these prions. In vitro, these prion proteins form amyloid fibrils spontaneously. The introduction of such fibrils made from Ure2p or Sup35p into yeast cells leads to the prion phenotypes [URE3] and [PSI], respectively. Previous studies on evolutionary biology of yeast prions have clearly established that [URE3] is not well conserved in the hemiascomycetous yeasts and particularly in S. paradoxus. Here we demonstrated that the S. paradoxus Ure2p is able to form infectious amyloid. These fibrils are more resistant than S. cerevisiae Ure2p fibrils to shear force. The observation, in vivo, of a distinct aggregation pattern for GFP fusions confirms the higher propensity of SpUre2p to form fibrillar structures. Our in vitro and in vivo analysis of aggregation propensity of the S. paradoxus Ure2p provides an explanation for its loss of infective properties and suggests that this protein belongs to the non-prion amyloid world.

Received for publication, September 7, 2006 , and in revised form, December 22, 2006.

^* This work was supported by grants from GIS "Infections à Prions" (to C. C.) and by the Natural Science Foundation of China (30470363, 30670428, 30620130109), the Chinese Ministry of Science and Technology (2006CB500703, 2006CB910903), the Chinese Academy of Sciences Knowledge Innovation Project (KSCX2-SW214-3), and by core funding from the Institute of Biophysics (to S. P.). 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.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Figs. S1–S5 and Table S1.

¹ Both authors contributed equally.

² To whom correspondence may be addressed. Tel.: 86-10-6485-6727; Fax: 86-10-6487-2026; E-mail: sarah.perrett{at}iname.com. ³ To whom correspondence may be addressed. Tel.: 33-556-999-017; Fax: 33-556-999-01; E-mail: Christophe.Cullin{at}ibgc.u-bordeaux2.fr.

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				M. Crapeau, C. Marchal, C. Cullin, and L. Maillet The Cellular Concentration of the Yeast Ure2p Prion Protein Affects Its Propagation as a Prion Mol. Biol. Cell, April 15, 2009; 20(8): 2286 - 2296. [Abstract] [Full Text] [PDF]