The mechanism of prion inhibition by HET-S.

  title={The mechanism of prion inhibition by HET-S.},
  author={Jason Greenwald and Carolin Buhtz and Christiane Ritter and Witek Kwiatkowski and Senyon Choe and M. L. Maddelein and Fr{\'e}d{\'e}rique Ness and Sandra Cescau and Alice Soragni and Dominik Leitz and Sven J. Saupe and Roland Riek},
  journal={Molecular cell},
  volume={38 6},
HET-S (97% identical to HET-s) has an N-terminal globular domain that exerts a prion-inhibitory effect in cis on its own prion-forming domain (PFD) and in trans on HET-s prion propagation. We show that HET-S fails to form fibrils in vitro and that it inhibits HET-s PFD fibrillization in trans. In vivo analyses indicate that beta-structuring of the HET-S PFD is required for HET-S activity. The crystal structures of the globular domains of HET-s and HET-S are highly similar, comprising a helical… CONTINUE READING