Effect of charged residues in the N-domain of Sup35 protein on prion [PSI+] stability and propagation

Abstract

Background:The prion domain (PrD) of Sup35p can aggregate to form the [PSI+] prion. Results:Introduction of charged lysine residues (sup35KK) in the Sup35p PrD alters prion properties. Conclusion:Some sup35KK alleles lead to the formation of new prion variants. Significance:Establishment of molecular interactions influencing [PSI +] prion stability and maintenance is a step toward an understanding of prion folding. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.