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Published online before print September 25, 2006, 10.1110/ps.062215206
Protein Science (2006), 15:2481-2487. Published by Cold Spring Harbor Laboratory Press. Copyright © 2006 The Protein Society
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Insights into the architecture of the Ure2p yeast protein assemblies from helical twisted fibrils

Neil Ranson1, Thusnelda Stromer2,4, Luc Bousset3,4, Ronald Melki3, and Louise C. Serpell2

1 Astbury Centre for Structural Molecular Biology & Institute for Molecular and Cellular Biology, University of Leeds, Leeds LS2 9JT, United Kingdom
2 Department of Biochemistry, University of Sussex, John Maynard Smith Building, Falmer BN1 9QG, United Kingdom
3 Laboratoire d'Enzymologie et Biochimie Structurales, CNRS, 91198 Gif-sur-Yvette Cedex, France

(RECEIVED March 14, 2006; FINAL REVISION August 4, 2006; ACCEPTED August 12, 2006)

The protein Ure2 from baker's yeast is associated with a heritable and transmissible phenotypic change in the yeast Saccharomyces cerevisiae. Such prion properties are thought to arise from the fact that Ure2p is able to self-assemble into insoluble fibrils. Assemblies of Ure2p are composed of full-length proteins in which the structure of the globular, functional, C-terminal domain is retained. We have carried out structural studies on full-length, wild-type Ure2p fibrils with a regularly twisted morphology. Using electron microscopy and cryo-electron microscopy with image analysis we show high-resolution images of the twisted filaments revealing details within the fibrillar structure. We examine these details in light of recent proposed models and discuss how this new information contributes to an understanding of the architecture of Ure2p yeast prion fibrils.

Keywords: prion protein; yeast; structure; fibrils; electron microscopy; image analysis


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J. Savistchenko, J. Krzewska, N. Fay, and R. Melki
Molecular Chaperones and the Assembly of the Prion Ure2p in Vitro
J. Biol. Chem., June 6, 2008; 283(23): 15732 - 15739.
[Abstract] [Full Text] [PDF]


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