Re-dissolving protein aggregates is crucial to cells, but the molecular basis has remained untested in direct experiments. Using combined optical tweezers and single-molecule fluo- rescence detection, we show that the disaggregase ClpB ex- trudes loops of protein chains through its central pore, and hence forcibly extracts protein chains from aggregates. The data reveal notable processivity, power, step-dynamics, and switching between translocation modes. Protein disaggre- gation can thus be highly deterministic and energy-driven process, while polypeptide loop extrusion may be exploited by other systems including p97/cdc48

,
Springer Science
doi.org/10.1007/s00249-021-01558-w
Eur. Biophys. J.
Biophysics

Tans, S.J. (2021). Polypeptide loop translocation by single ClpB disaggregases. In Eur. Biophys. J. (Vol. 50, pp. 55–55). Springer Science. doi:10.1007/s00249-021-01558-w