Solid-state NMR spectroscopy reveals that E. coli inclusion bodies of HET-s(218-289) are amyloids.
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.
Wasmer
Christian
C
Laboratorium für Physikalische Chemie, ETH Zurich, 8093 Zurich, Switzerland.
Benkemoun
Laura
L
Sabaté
Raimon
R
Steinmetz
Michel O
MO
Coulary-Salin
Bénédicte
B
Wang
Lei
L
Riek
Roland
R
Saupe
Sven J
SJ
Meier
Beat H
BH
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
D000682:Amyloid; D005656:Fungal Proteins; C083891:HET-S protein, Podospora anserina; D011328:Prions; D011994:Recombinant Proteins