Fig 5. Identification of three Sup35 states in E. coli.
In summary, Sup35 aggregates could form a complex with cytoplasmic HSP90 and Dna K in E. coli , and a stable monomer also existed (Figure 5). The aggregate state was maintained by a complex, which was composed of non-equilibrium bindings of molecular chaperones. In addition, the Sup35 complex exhibited an aggregate morphology different from the Sup35 fibrils formed in vitro . Further studies are underway to elucidate the different regulatory mechanisms underlying prion assembly in E. coli and yeast.