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. 2004 Nov 24;119(5):653-65.
doi: 10.1016/j.cell.2004.11.027.

Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB

Jimena Weibezahn  1 , Peter Tessarz, Christian Schlieker, Regina Zahn, Zeljka Maglica, Sukyeong Lee, Hanswalter Zentgraf, Eilika U Weber-Ban, David A Dougan, Francis T F Tsai, Axel Mogk, Bernd Bukau
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Free article

Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB

Jimena Weibezahn et al. Cell. .
Free article

Abstract

Cell survival under severe thermal stress requires the activity of the ClpB (Hsp104) AAA+ chaperone that solubilizes and reactivates aggregated proteins in concert with the DnaK (Hsp70) chaperone system. How protein disaggregation is achieved and whether survival is solely dependent on ClpB-mediated elimination of aggregates or also on reactivation of aggregated proteins has been unclear. We engineered a ClpB variant, BAP, which associates with the ClpP peptidase and thereby is converted into a degrading disaggregase. BAP translocates substrates through its central pore directly into ClpP for degradation. ClpB-dependent translocation is demonstrated to be an integral part of the disaggregation mechanism. Protein disaggregation by the BAP/ClpP complex remains dependent on DnaK, defining a role for DnaK at early stages of the disaggregation reaction. The activity switch of BAP to a degrading disaggregase does not support thermotolerance development, demonstrating that cell survival during severe thermal stress requires reactivation of aggregated proteins.

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