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.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Amyloid / chemistry*
-
Amyloid / metabolism
-
Escherichia coli / genetics
-
Escherichia coli / metabolism*
-
Fungal Proteins / chemistry*
-
Fungal Proteins / metabolism
-
Inclusion Bodies / chemistry*
-
Inclusion Bodies / metabolism
-
Nuclear Magnetic Resonance, Biomolecular
-
Prions / chemistry
-
Prions / metabolism
-
Recombinant Proteins / chemistry
-
Recombinant Proteins / metabolism
Substances
-
Amyloid
-
Fungal Proteins
-
HET-S protein, Podospora anserina
-
Prions
-
Recombinant Proteins