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Journal Article

The [PSI+] prion and HSP104 modulate cytochrome c oxidase deficiency caused by deletion of COX12


Stewart,  J.
Stewart – Mitochondrial Mutations and Genome Co-evolution, Research Groups, Max Planck Institute for Biology of Ageing, Max Planck Society;

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Saini, P. K., Dawitz, H., Aufschnaiter, A., Thomas, J., Amblard, A., Stewart, J., et al. (2021). The [PSI+] prion and HSP104 modulate cytochrome c oxidase deficiency caused by deletion of COX12. bioRxiv, 2021.10.08.463630. doi:10.1101/2021.10.08.463630.

Cite as: https://hdl.handle.net/21.11116/0000-000A-F8ED-4
Cytochrome c oxidase is a pivotal enzyme of the mitochondrial respiratory chain, which sustains bioenergetics of eukaryotic cells. Cox12, a peripheral subunit of cytochrome c oxidase, is required for full activity of the enzyme, but its exact function is unknown. Here, experimental evolution of a Saccharomyces cerevisiae Δcox12 strain for ~300 generations allowed to restore the activity of cytochrome c oxidase. In one population, the enhanced bioenergetics was caused by a A375V mutation in the AAA+ disaggregase Hsp104. Deletion or overexpression of Hsp104 also increased respiration of the Δcox12 ancestor strain. This beneficial effect of Hsp104 was related to the loss of the [PSI+] prion, which forms cytosolic amyloid aggregates of the Sup35 protein. Overall, our data demonstrate that cytosolic aggregation of a prion impairs the mitochondrial metabolism of cells defective for Cox12. These findings identify a new functional connection between cytosolic proteostasis and biogenesis of the mitochondrial respiratory chain.Competing Interest StatementThe authors have declared no competing interest.