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
Eur. Biophys. J. with Biophysics Letters

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