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Updated: Apr 12, 2026

Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions
Published on: June 7, 2020
Quantifying the role of chaperones in protein translocation by computational modeling
Salvatore Assenza1, Paolo De Los Rios1, Alessandro Barducci1
1Laboratoire de Biophysique Statistique, Ecole Polytechnique Fédérale de Lausanne Lausanne, Switzerland.
Abstract:
The molecular chaperone Hsp70 plays a central role in the import of cytoplasmic proteins into organelles, driving their translocation by binding them from the organellar interior. Starting from the experimentally-determined structure of the E. coli Hsp70, we computed, by means of molecular simulations, the effective free-energy profile for substrate translocation upon chaperone binding. We then used the resulting free energy to quantitatively characterize the kinetics of the import process, whose comparison with unassisted translocation highlights the essential role played by Hsp70 in importing cytoplasmic proteins.
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