TY - JOUR TI - Prion propagation can occur in a prokaryote and requires the ClpB chaperone AU - Yuan, Andy H AU - Garrity, Sean J AU - Nako, Entela AU - Hochschild, Ann A2 - Greenberg, Peter VL - 3 PY - 2014 DA - 2014/08/13 SP - e02949 C1 - eLife 2014;3:e02949 DO - 10.7554/eLife.02949 UR - https://doi.org/10.7554/eLife.02949 AB - Prions are self-propagating protein aggregates that are characteristically transmissible. In mammals, the PrP protein can form a prion that causes the fatal transmissible spongiform encephalopathies. Prions have also been uncovered in fungi, where they act as heritable, protein-based genetic elements. We previously showed that the yeast prion protein Sup35 can access the prion conformation in Escherichia coli. Here, we demonstrate that E. coli can propagate the Sup35 prion under conditions that do not permit its de novo formation. Furthermore, we show that propagation requires the disaggregase activity of the ClpB chaperone. Prion propagation in yeast requires Hsp104 (a ClpB ortholog), and prior studies have come to conflicting conclusions about ClpB's ability to participate in this process. Our demonstration of ClpB-dependent prion propagation in E. coli suggests that the cytoplasmic milieu in general and a molecular machine in particular are poised to support protein-based heredity in the bacterial domain of life. KW - prion KW - chaperone KW - Sup35 KW - ClpB KW - protein-based heredity JF - eLife SN - 2050-084X PB - eLife Sciences Publications, Ltd ER -