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Solid-state NMR sequential assignments of the amyloid core of full-length Sup35p

Schütz, Anne ; Habenstein, Birgit ; Luckgei, Nina ; Bousset, Luc ; Sourigues, Yannick ; Nielsen, Anders ; Melki, Ronald ; Böckmann, Anja ; Meier, Beat

In: Biomolecular NMR Assignments, 2014, vol. 8, no. 2, p. 349-356

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    Title
    • Solid-state NMR sequential assignments of the amyloid core of full-length Sup35p
    Author
    • Schütz, Anne. Physical Chemistry, ETH Zürich, Wolfgang-Pauli-Strasse 10, 8093, Zurich, Switzerland
    • Habenstein, Birgit. Institut de Biologie et Chimie des Protéines, UMR 5086 CNRS/Université de Lyon 1, 7 passage du Vercors, 69367, Lyon, France
    • Luckgei, Nina. Institut de Biologie et Chimie des Protéines, UMR 5086 CNRS/Université de Lyon 1, 7 passage du Vercors, 69367, Lyon, France
    • Bousset, Luc. Laboratoire d'Enzymologie et Biochimie Structurales, UPR 3082 CNRS, Avenue de la Terrasse, 91198, Gif-sur-Yvette, France
    • Sourigues, Yannick. Laboratoire d'Enzymologie et Biochimie Structurales, UPR 3082 CNRS, Avenue de la Terrasse, 91198, Gif-sur-Yvette, France
    • Nielsen, Anders. Physical Chemistry, ETH Zürich, Wolfgang-Pauli-Strasse 10, 8093, Zurich, Switzerland
    • Melki, Ronald. Laboratoire d'Enzymologie et Biochimie Structurales, UPR 3082 CNRS, Avenue de la Terrasse, 91198, Gif-sur-Yvette, France
    • Böckmann, Anja. Institut de Biologie et Chimie des Protéines, UMR 5086 CNRS/Université de Lyon 1, 7 passage du Vercors, 69367, Lyon, France
    • Meier, Beat. Physical Chemistry, ETH Zürich, Wolfgang-Pauli-Strasse 10, 8093, Zurich, Switzerland
    Document Type
    • Postprint
    OAI-PMH Identifier
    • oai:doc.rero.ch:326264
    Summary
    Sup35p is a yeast prion and is responsible for the [PSI +] trait in Saccharomyces cerevisiae. With 685 amino acids, full-length soluble and fibrillar Sup35p are challenging targets for structural biology as they cannot be investigated by X-ray crystallography or NMR in solution. We present solid-state NMR studies of fibrils formed by the full-length Sup35 protein. We detect an ordered and rigid core of the protein that gives rise to narrow and strong peaks, while large parts of the protein show either static disorder or dynamics on time scales which interfere with dipolar polarization transfer or shorten the coherence lifetime. Thus, only a small subset of resonances is observed in 3D spectra. Here we describe in detail the sequential assignments of the 22 residues for which resonances are observed in 3D spectra: their chemical shifts mostly corresponding to β-sheet secondary structure. We suspect that these residues form the amyloid core of the fibril.