2021-07-01
Polypeptide loop translocation by single ClpB disaggregases
Publication
Publication
Eur. Biophys. J. with Biophysics Letters , Volume 50 - Issue S1 p. 55- 55
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
| Additional Metadata | |
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| , | |
| Springer Science and Business Media LLC | |
| doi.org/10.1007/s00249-021-01558-w | |
| Eur. Biophys. J. with Biophysics Letters | |
| Organisation | Biophysics |
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Tans, S. (2021). Polypeptide loop translocation by single ClpB disaggregases. Eur. Biophys. J. With Biophysics Letters, 50(S1), 55–55.https://doi.org/10.1007/s00249-021-01558-w |
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