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A Native-Like Conformation for the C-Terminal Domain of the Prion Ure2p within its Fibrillar Form

Authors

  • Dr. Birgit Habenstein,

    1. Institut de Biologie et Chimie des Protéines, UMR 5086 CNRS/Université de Lyon 1, 7 passage du Vercors, 69367 Lyon (France)
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    • These authors contributed equally to this work.

  • Dr. Luc Bousset,

    1. Laboratoine d'Enzymologie et Biochimie Structurale, UPR 3082 CNRS, Avenue de la Terrasse, 91198 Gif-sur-Yvette (France)
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    • These authors contributed equally to this work.

  • Yannick Sourigues,

    1. Laboratoine d'Enzymologie et Biochimie Structurale, UPR 3082 CNRS, Avenue de la Terrasse, 91198 Gif-sur-Yvette (France)
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  • Dr. Mehdi Kabani,

    1. Laboratoine d'Enzymologie et Biochimie Structurale, UPR 3082 CNRS, Avenue de la Terrasse, 91198 Gif-sur-Yvette (France)
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  • Dr. Antoine Loquet,

    1. Institut de Biologie et Chimie des Protéines, UMR 5086 CNRS/Université de Lyon 1, 7 passage du Vercors, 69367 Lyon (France)
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  • Prof. Dr. Beat H. Meier,

    Corresponding author
    1. Physical Chemistry, ETH Zürich, Wolfgang-Pauli-Strasse 10, 8093 Zürich (Switzerland)
    • Physical Chemistry, ETH Zürich, Wolfgang-Pauli-Strasse 10, 8093 Zürich (Switzerland)
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  • Dr. Ronald Melki,

    Corresponding author
    1. Laboratoine d'Enzymologie et Biochimie Structurale, UPR 3082 CNRS, Avenue de la Terrasse, 91198 Gif-sur-Yvette (France)
    • Laboratoine d'Enzymologie et Biochimie Structurale, UPR 3082 CNRS, Avenue de la Terrasse, 91198 Gif-sur-Yvette (France)
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  • Dr. Anja Böckmann

    Corresponding author
    1. Institut de Biologie et Chimie des Protéines, UMR 5086 CNRS/Université de Lyon 1, 7 passage du Vercors, 69367 Lyon (France)
    • Institut de Biologie et Chimie des Protéines, UMR 5086 CNRS/Université de Lyon 1, 7 passage du Vercors, 69367 Lyon (France)
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  • This work was supported by the Agence Nationale de la Recherche (ANR-07-PCVI-0013-03, ANR-06-BLAN-0266, ANR-PCV08 321323, and ANR08-PCVI-0022-02), the ETH Zurich, the Swiss National Science Foundation (Grant 200020_124611), and the Centre National de la Recherche Scientifique. We acknowledge support from the Partenariat Hubert Curien Germaine de Staël. We also acknowledge support from the European Commission under the Seventh Framework Programme (FP7), contract Bio-NMR 261863. We also thank Dr. Christian Wasmer for help in setting up the experiments.

Abstract

original image

Taking a definite stance: Protein fibrils are often associated with disorder and polymorphism, but the prion fibrils of Ure2p are shown (through solid-state NMR spectroscopy) to be highly ordered, and the conformations of the globular domain to be more restricted within the fibrils (black; see scheme) than in Ure2p single crystals (red). This finding implies that steric impairment is at the origin of the [URE3] phenotype in yeast.

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