Yeast [PSI+] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104.
The yeast [PSI+] determinant is related to formation of large prion-like aggregates of the conformationally altered Sup35 protein. Here, we show that these aggregates are composed of small Sup35 prion polymers and associated proteins. In contrast to other protein complexes of yeast lysates, but similarly to amyloid fibers, these polymers are insoluble in SDS at room temperature. The polymers on average are about 30-fold smaller than the aggregates and comprise from 8 to 50 Sup35 monomers. The size of polymers is characteristic of a given [PSI+] variant and differs between the variants. Blocked expression of Hsp104 chaperone causes gradual increase in the size of prion polymers, while inactivation of Hsp104 by guanidine HCl completely stops their fragmentation, which shows indispensability of Hsp104 for this process.
D001704:Biopolymers / Q000378:metabolism*; D006360:Heat-Shock Proteins / Q000378:metabolism*; D010454:Peptide Termination Factors; D011328:Prions / Q000096:biosynthesis* / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000096:biosynthesis* / Q000378:metabolism*; D012967:Sodium Dodecyl Sulfate
D001704:Biopolymers; D006360:Heat-Shock Proteins; D010454:Peptide Termination Factors; D011328:Prions; C068068:SUP35 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; C070972:HsP104 protein, S cerevisiae; D012967:Sodium Dodecyl Sulfate