We describe a distant homologue of the fungal HET-s prion, which is found in the fungus Fusarium graminearum. The domain FgHET-s(218-289), which corresponds to the prion domain in HET-s from Podospora anserina, forms amyloid fibrils in vitro and is able to efficiently cross-seed HET-s(218-289) prion formation. We structurally characterize FgHET-s(218-289), which displays 38% sequence identity with HET-s(218-289). Solid-state NMR and hydrogen/deuterium exchange detected by NMR show that the fold and a number of structural details are very similar for the prion domains of the two proteins. This structural similarity readily explains why cross-seeding occurs here in spite of the sequence divergence. © 2010 Elsevier Ltd.
|Journal||Journal of Molecular Biology|
|Publication status||Published - 1 Sep 2010|
- FgHET-s protein
- HET-s protein