• DOI:10.1038/s41586-020-1964-y
Corpus ID: 210949475

Processive extrusion of polypeptide loops by a Hsp100 disaggregase

@article{Avellaneda2020ProcessiveEO,
  title={Processive extrusion of polypeptide loops by a Hsp100 disaggregase},
  author={Mario J. Avellaneda and Kamila B. Franke and Vanda Sunderlikova and B. Bukau and A. Mogk and S. Tans},
  journal={Nature},
  year={2020},
  volume={578},
  pages={317-320}
}

Mario J. Avellaneda, Kamila B. Franke, +3 authors S. Tans

Published 2020

Chemistry, Medicine, Computer Science

Nature

The ability to reverse protein aggregation is vital to cells 1 , 2 . Hsp100 disaggregases such as ClpB and Hsp104 are proposed to catalyse this reaction by translocating polypeptide loops through their central pore 3 , 4 . This model of disaggregation is appealing, as it could explain how polypeptides entangled within aggregates can be extracted and subsequently refolded with the assistance of Hsp70 4 , 5 . However, the model is also controversial, as the necessary motor activity has not been… CONTINUE READING

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