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Updated: Aug 7, 2026

Intracellular Refolding Assay
Published on: January 24, 2012
Heat Shock Proteins in the "Hot" Mitochondrion: Identity and Putative Roles
Mohamed A Nasr1,2, Galina I Dovbeshko3, Stephen L Bearne4,5
1Department of Chemistry and Physics, Mount Saint Vincent University, Halifax, Nova Scotia, B3M 2J6, Canada.
Abstract:
The mitochondrion is known as the "powerhouse" of eukaryotic cells since it is the main site of adenosine 5'-triphosphate (ATP) production. Using a temperature-sensitive fluorescent probe, it has recently been suggested that the stray free energy, not captured into ATP, is potentially sufficient to sustain mitochondrial temperatures higher than the cellular environment, possibly reaching up to 50 °C. By 50 °C, some DNA and mitochondrial proteins may reach their melting temperatures; how then do these biomolecules maintain their structure and function? Further, the production of reactive oxygen species (ROS) accelerates with temperature, implying higher oxidative stresses in the mitochondrion than generally appreciated. Herein, it is proposed that mitochondrial heat shock proteins (particularly Hsp70), in addition to their roles in protein transport and folding, protect mitochondrial proteins and DNA from thermal and ROS damage. Other thermoprotectant mechanisms are also discussed.
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