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Hsp70 chaperones use ATP to remodel native protein oligomers and stable aggregates by entropic pulling

Nature Structural & Molecular Biology volume 23, pages 766–769 (2016)Cite this article

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Forceful unfolding by entropic pulling is the general mechanism by which Hsp70 and Hsp110 chaperones control the oligomeric states, structures and activities of cellular proteins.

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Figure 1: The free energy originating from the steric clashes between the obstacle and Hsp70, ΔGEP, decreases with the number of amino acids between the obstacle (here a membrane pore) and the Hsp70-binding site (blue line with solid circles).
Figure 2: Members of the Hsp70 chaperone family use ATP hydrolysis to recruit a universal entropic pulling mechanism to unfold and translocate nascent polypeptides, disaggregate misfolded proteins and disentangle native protein oligomers in the cell.

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Authors and Affiliations

  1. Paolo De Los Rios is at the Institute of Physics, School of Basic Sciences and Institute of Bioengineering, School of Life Sciences, Ecole Polytechnique Fédérale de Lausanne (EPFL), Lausanne, Switzerland.,

    Paolo De Los Rios

  2. Pierre Goloubinoff is at the Department of Plant Molecular Biology, Faculty of Biology and Medicine, University of Lausanne, Lausanne, Switzerland.,

    Pierre Goloubinoff

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  1. Paolo De Los Rios
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  2. Pierre Goloubinoff
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Correspondence to Pierre Goloubinoff.

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De Los Rios, P., Goloubinoff, P. Hsp70 chaperones use ATP to remodel native protein oligomers and stable aggregates by entropic pulling. Nat Struct Mol Biol 23, 766–769 (2016). https://doi.org/10.1038/nsmb.3283

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