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Solid‐State NMR Spectroscopy Reveals that E. coli Inclusion Bodies of HET‐s(218–289) are Amyloids |
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| Authors: | Christian Wasmer Laura Benkemoun Dr. Raimon Sabaté Dr. Michel O. Steinmetz Dr. Bénédicte Coulary‐Salin Dr. Lei Wang Dr. Roland Riek Prof. Sven J. Saupe Dr. Beat H. Meier Prof. |
| Affiliation: | 1. Laboratorium für Physikalische Chemie, ETH Zurich, 8093 Zurich (Switzerland), Fax: (+41)?446‐321‐621;2. Laboratoire de Génétique Moléculaire des Champignons, IBGC UMR 5095 CNRS, Université de Bordeaux 2, Bordeaux (France);3. Biomolecular Research, Structural Biology, Paul Scherrer Institut, 5232 Villigen (Switzerland) |
| Abstract: | Protein deposition frequently occurs as inclusion bodies (IBs) during heterologous protein expression in E. coli. The structure of these E. coli IBs of the prion‐forming domain from the fungal prion HET‐s is the same as that previously determined for fibrils assembled in vitro, and show prion infectivity. These results demonstrate that the IBs of HET‐s(218–289) are amyloids.  |
| Keywords: | amyloids inclusion bodies NMR spectroscopy proteins structure elucidation |