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Open AccessArticle

ClpG Provides Increased Heat Resistance by Acting as Superior Disaggregase

Center for Molecular Biology of the University of Heidelberg (ZMBH) and German Cancer Research Center (DKFZ), DKFZ-ZMBH Alliance, 69120 Heidelberg, Germany
Department of Microbiology, Tumor and Cell Biology, Karolinska Institute, 17177 Stockholm, Sweden
Author to whom correspondence should be addressed.
These authors contributed equally to this work.
Biomolecules 2019, 9(12), 815;
Received: 27 October 2019 / Revised: 27 November 2019 / Accepted: 28 November 2019 / Published: 2 December 2019
Elevation of temperature within and above the physiological limit causes the unfolding and aggregation of cellular proteins, which can ultimately lead to cell death. Bacteria are therefore equipped with Hsp100 disaggregation machines that revert the aggregation process and reactivate proteins otherwise lost by aggregation. In Gram-negative bacteria, two disaggregation systems have been described: the widespread ClpB disaggregase, which requires cooperation with an Hsp70 chaperone, and the standalone ClpG disaggregase. ClpG co-exists with ClpB in selected bacteria and provides superior heat resistance. Here, we compared the activities of both disaggregases towards diverse model substrates aggregated in vitro and in vivo at different temperatures. We show that ClpG exhibits robust activity towards all disordered aggregates, whereas ClpB acts poorly on the protein aggregates formed at very high temperatures. Extreme temperatures are expected not only to cause extended protein unfolding, but also to result in an accelerated formation of protein aggregates with potentially altered chemical and physical parameters, including increased stability. We show that ClpG exerts higher threading forces as compared to ClpB, likely enabling ClpG to process “tight” aggregates formed during severe heat stress. This defines ClpG as a more powerful disaggregase and mechanistically explains how ClpG provides increased heat resistance.
Keywords: protein disaggregation; heat resistance; chaperone; protein aggregation; AAA protein, Hsp100 protein disaggregation; heat resistance; chaperone; protein aggregation; AAA protein, Hsp100
MDPI and ACS Style

Katikaridis, P.; Meins, L.; Kamal, S.M.; Römling, U.; Mogk, A. ClpG Provides Increased Heat Resistance by Acting as Superior Disaggregase. Biomolecules 2019, 9, 815.

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