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.