J‐protein requirements of multiple [PSI+] prion variants in two distinct yeast strains

Abstract

The objective of this study was to determine the importance of prion variant and yeast strain variation on prion chaperone requirements. The J‐protein Sis1 and the prion [PSI+] were used as a model system to explore the impact of amyloid conformation (prion variants) and yeast strain polymorphisms (yeast genetic background) on chaperone requirements. The primary method used in this study was complementation by plasmid‐shuffling in the budding yeast Saccharomyces cerevisiae.Summary of ResultsYeast strain background had a small but noticeable effect on chaperone requirements; this effect is likely due primarily to altered chaperone protein levels between strains. While many prion variants shared similar chaperone requirements, some significant differences were found.ConclusionsJ‐protein chaperone requirements are significantly determined by the specific amyloid conformation of a yeast prion but relatively unaffected by yeast genetic background. Funding for this research was provided by Lafayette College in the form of the EXCEL Scholars program, Department of Chemistry research funds, and start‐up funds provided for JKH.