title: Solid-state NMR spectroscopy reveals that E. coli inclusion bodies of HET-s(218-289) are amyloids.
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.
authors.affiliation: Laboratorium für Physikalische Chemie, ETH Zurich, 8093 Zurich, Switzerland.
authors.forename: Christian
authors.initials: C
authors.lastname: Wasmer
authors.forename: Laura
authors.initials: L
authors.lastname: Benkemoun
authors.forename: Raimon
authors.initials: R
authors.lastname: Sabaté
authors.forename: Michel O
authors.initials: MO
authors.lastname: Steinmetz
authors.forename: Bénédicte
authors.initials: B
authors.lastname: Coulary-Salin
authors.forename: Lei
authors.initials: L
authors.lastname: Wang
authors.forename: Roland
authors.initials: R
authors.lastname: Riek
authors.forename: Sven J
authors.initials: SJ
authors.lastname: Saupe
authors.forename: Beat H
authors.initials: BH
authors.lastname: Meier
mesh_terms: D000682:Amyloid / Q000737:chemistry* / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D005656:Fungal Proteins / Q000737:chemistry* / Q000378:metabolism; D002479:Inclusion Bodies / Q000737:chemistry* / Q000378:metabolism; D019906:Nuclear Magnetic Resonance, Biomolecular; D011328:Prions / Q000737:chemistry / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism
chemical_list: D000682:Amyloid; D005656:Fungal Proteins; C083891:HET-S protein, Podospora anserina; D011328:Prions; D011994:Recombinant Proteins