Chaperone networks in protein disaggregation and prion propagation.

@article{Winkler2012ChaperoneNI,
  title={Chaperone networks in protein disaggregation and prion propagation.},
  author={Juliane Winkler and Jens Tyedmers and Bernd Bukau and Axel Mogk},
  journal={Journal of structural biology},
  year={2012},
  volume={179 2},
  pages={152-60}
}
The oligomeric AAA+ chaperones Escherichia coli ClpB and Saccharomyces cerevisiae Hsp104 cooperate with cognate Hsp70/Hsp40 chaperone machineries in the reactivation of aggregated proteins in E. coli and S. cerevisiae. In addition, Hsp104 and Hsp70/Hsp40 are crucial for the maintenance of prion aggregates in yeast cells. While the bichaperone system efficiently solubilizes stress-generated amorphous aggregates, structurally highly ordered prion fibrils are only partially processed, resulting in… CONTINUE READING