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

Saini, P. K.; Dawitz, H.; Aufschnaiter, A.; Thomas, J.; Amblard, A.; Stewart, J.; Thierry-Mieg, N.; Ott, M.; Pierrel, F.

doi:10.1101/2021.10.08.463630

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

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

MPS-Authors

/persons/resource/persons129358

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

External Resource

https://www.biorxiv.org/content/biorxiv/early/2021-10-18/2021.10.08.463630.full.pdf
(Any fulltext)

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

There are no public fulltexts stored in PuRe

Supplementary Material (public)

There is no public supplementary material available

Citation

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

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 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.