Structural similarity between the prion domain of HET-s and a homologue can explain amyloid cross-seeding in spite of limited sequence identity

Christian Wasmer, Agnes Zimmer, Raimon Sabaté, Alice Soragni, Sven J. Saupe, Christiane Ritter, Beat H. Meier

Research output: Contribution to journalArticleResearchpeer-review

39 Citations (Scopus)

Abstract

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.
Original languageEnglish
Pages (from-to)311-325
JournalJournal of Molecular Biology
Volume402
Issue number2
DOIs
Publication statusPublished - 1 Sep 2010

Keywords

  • Amyloid
  • FgHET-s protein
  • Fibrils
  • HET-s protein
  • Prion

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