Distinct amino acid compositional requirements for formation and maintenance of the [PSI⁺] prion in yeast.

ABSTRACT: Multiple yeast prions have been identified that result from the structural conversion of proteins into a self-propagating amyloid form. Amyloid-based prion activity in yeast requires a series of discrete steps. First, the prion protein must form an amyloid nucleus that can recruit and structurally convert additional soluble proteins. Subsequently, maintenance of the prion during cell division requires fragmentation of these aggregates to create new heritable propagons. For the Saccharomyces cerevisiae prion protein Sup35, these different activities are encoded by different regions of the Sup35 prion domain. An N-terminal glutamine/asparagine-rich nucleation domain is required for nucleation and fiber growth, while an adjacent oligopeptide repeat domain is largely dispensable for prion nucl

SUBMITTER: MacLea KS 

PROVIDER: S-EPMC4323492 | biostudies-literature | 2015 Mar

REPOSITORIES: biostudies-literature