Conformational change of glutathione-S-transferase by its co-expression with prion domain of yeast Ure2p

摘要

The Ure2 protein from Saccharomyces cerevisisae has a changeable structure similar to that of mam- malian prion protein. Its N-terminal is the prion domain (PrD) consisting of 65 amino acids which plays a critical role in yeast prion development. In this study, PrD gene was recombinated with glutathione-S-transferase (GST) gene, and a soluble GST-PrD (aGST-PrD) fusion protein was expressed in E. coli.