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The [PSI+] prion and HSP104 modulate cytochrome c oxidase deficiency caused by deletion of COX12
Abstract : ABSTRACT 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 Δ cox12 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 Δ cox12 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.
https://hal.archives-ouvertes.fr/hal-03402829
Contributeur : Fabien Pierrel Connectez-vous pour contacter le contributeur
Soumis le : jeudi 4 novembre 2021 - 17:05:43
Dernière modification le : lundi 22 novembre 2021 - 15:18:01
Contributeur : Fabien Pierrel Connectez-vous pour contacter le contributeur
Soumis le : jeudi 4 novembre 2021 - 17:05:43
Dernière modification le : lundi 22 novembre 2021 - 15:18:01
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Dcox12 V11b.pdf
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