Solid-state NMR spectroscopy reveals that E. coli inclusion bodies of HET-s(218-289) are amyloids

Angew Chem Int Ed Engl. 2009;48(26):4858-60. doi: 10.1002/anie.200806100.

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