Polypeptide loop translocation by single ClpB disaggregases

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Publication date
DOI http://dx.doi.org/10.1007/s00249-021-01558-w
Reference S.J. Tans, Polypeptide loop translocation by single ClpB disaggregases, Eur. Biophys. J. with Biophysics Letters 50, (S1), 55-55 (2021)
Group Biophysics

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