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The [PSI+] prion modulates cytochrome c oxidase deficiency caused by deletion of COX12

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

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Zitation

Saini, P. K., Dawitz, H., Aufschnaiter, A., Bondarev, S., Thomas, J., Amblard, A., et al. (2022). The [PSI+] prion modulates cytochrome c oxidase deficiency caused by deletion of COX12. Mol Biol Cell, mbcE21100499. doi:10.1091/mbc.E21-10-0499.


Zitierlink: https://hdl.handle.net/21.11116/0000-000B-B6A1-1
Zusammenfassung
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 Deltacox12 strain for approximately 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 Deltacox12 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.