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- Title
Strains of [PSI<sup>+</sup>] are distinguished by their efficiencies of prion-mediated conformational conversion.
- Authors
Uptain, Susan M.; Sawicki, George J.; Caughey, Byron; Lindquist, Susan
- Abstract
Yeast prions are protein-based genetic elements that produce phenotypes through self-perpetuating changes in protein conformation. For the prion [PSI+] this protein is Sup35, which is comprised of a priondetermining region (NM) fused to a translational termination region. [PSI+] strains (variants) with different heritable translational termination defects (weak or strong) can exist in the same genetic background. [PSI+] variants are reminiscent of mammalian prion strains, which can be passaged in the same mouse strain yet have different disease latencies and brain pathologies. We found that [PSI+] variants contain different ratios of Sup35 in the prion and nonprion state that correlate with different translation termination efficiencies. Indeed, the partially purified prion form of Sup35 from a strong [PSI+] variant converted purified NM much more efficiently than that of several weak variants. However, this difference was lost in a second round of conversion in vitro. Thus, [PSI+] variants result from differences in the efficiency of prion-mediated conversion, and the maintenance of [PSI+] variants involves more than nucleated conformational conversion (templating) to NM alone.
- Publication
EMBO Journal, 2001, Vol 20, Issue 22, p6236
- ISSN
0261-4189
- Publication type
Academic Journal
- DOI
10.1093/emboj/20.22.6236