Probing the role of PrP repeats in conformational conversion and amyloid assembly of chimeric yeast prions.

ABSTRACT: Oligopeptide repeats appear in many proteins that undergo conformational conversions to form amyloid, including the mammalian prion protein PrP and the yeast prion protein Sup35. Whereas the repeats in PrP have been studied more exhaustively, interpretation of these studies is confounded by the fact that many details of the PrP prion conformational conversion are not well understood. On the other hand, there is now a relatively good understanding of the factors that guide the conformational conversion of the Sup35 prion protein. To provide a general model for studying the role of oligopeptide repeats in prion conformational conversion and amyloid formation, we have substituted various numbers of the PrP octarepeats for the endogenous Sup35 repeats. The resulting chimeric proteins can adopt

SUBMITTER: Dong J 

PROVIDER: S-EPMC2262835 | biostudies-literature | 2007 Nov

REPOSITORIES: biostudies-literature