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The [PSI+] prion modulates cytochrome c oxidase deficiency caused by deletion of COX12. / Saini, Pawan Kumar; Dawitz, Hannah; Aufschnaiter, Andreas; Bondarev, Stanislav ; Thomas, Jinsu; Amblard, Amélie; Stewart, James; Thierry-Mieg, Nicolas; Ott, Martin; Pierrel, Fabien.

In: Molecular Biology of the Cell, Vol. 33, No. 14, 01.12.2022, p. ar130.

Research output: Contribution to journal › Article › peer-review

Harvard

Saini, PK, Dawitz, H, Aufschnaiter, A, Bondarev, S, Thomas, J, Amblard, A, Stewart, J, Thierry-Mieg, N, Ott, M & Pierrel, F 2022, 'The [PSI+] prion modulates cytochrome c oxidase deficiency caused by deletion of COX12', Molecular Biology of the Cell, vol. 33, no. 14, pp. ar130. https://doi.org/10.1091/mbc.E21-10-0499

APA

Saini, P. K., Dawitz, H., Aufschnaiter, A., Bondarev, S., Thomas, J., Amblard, A., Stewart, J., Thierry-Mieg, N., Ott, M., & Pierrel, F. (2022). The [PSI+] prion modulates cytochrome c oxidase deficiency caused by deletion of COX12. Molecular Biology of the Cell, 33(14), ar130. https://doi.org/10.1091/mbc.E21-10-0499

Vancouver

Saini PK, Dawitz H, Aufschnaiter A, Bondarev S, Thomas J, Amblard A et al. The [PSI+] prion modulates cytochrome c oxidase deficiency caused by deletion of COX12. Molecular Biology of the Cell. 2022 Dec 1;33(14):ar130. https://doi.org/10.1091/mbc.E21-10-0499

Author

Saini, Pawan Kumar ; Dawitz, Hannah ; Aufschnaiter, Andreas ; Bondarev, Stanislav ; Thomas, Jinsu ; Amblard, Amélie ; Stewart, James ; Thierry-Mieg, Nicolas ; Ott, Martin ; Pierrel, Fabien. / The [PSI+] prion modulates cytochrome c oxidase deficiency caused by deletion of COX12. In: Molecular Biology of the Cell. 2022 ; Vol. 33, No. 14. pp. ar130.

BibTeX

@article{0717ee9f153a4ba6a67b4ff15cbb5211,
title = "The [PSI+] prion modulates cytochrome c oxidase deficiency caused by deletion of COX12",
abstract = "Cytochrome c oxidase (CcO) is a pivotal enzyme of the mitochondrial respiratory chain, which sustains bioenergetics of eukaryotic cells. Cox12, a peripheral subunit of CcO 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 CcO oxidase. In one population, the enhanced bioenergetics was caused by a A375V mutation in the cytosolic 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.",
keywords = "Humans, Prions/genetics, Peptide Termination Factors/metabolism, Saccharomyces cerevisiae Proteins/genetics, Cytochrome-c Oxidase Deficiency, Heat-Shock Proteins/metabolism, Saccharomyces cerevisiae/metabolism, Electron Transport Complex IV/metabolism",
author = "Saini, {Pawan Kumar} and Hannah Dawitz and Andreas Aufschnaiter and Stanislav Bondarev and Jinsu Thomas and Am{\'e}lie Amblard and James Stewart and Nicolas Thierry-Mieg and Martin Ott and Fabien Pierrel",
year = "2022",
month = dec,
day = "1",
doi = "10.1091/mbc.E21-10-0499",
language = "English",
volume = "33",
pages = "ar130",
journal = "Molecular Biology of the Cell",
issn = "1059-1524",
publisher = "American Society for Cell Biology",
number = "14",

}

RIS

TY - JOUR

T1 - The [PSI+] prion modulates cytochrome c oxidase deficiency caused by deletion of COX12

AU - Saini, Pawan Kumar

AU - Dawitz, Hannah

AU - Aufschnaiter, Andreas

AU - Bondarev, Stanislav

AU - Thomas, Jinsu

AU - Amblard, Amélie

AU - Stewart, James

AU - Thierry-Mieg, Nicolas

AU - Ott, Martin

AU - Pierrel, Fabien

PY - 2022/12/1

Y1 - 2022/12/1

N2 - Cytochrome c oxidase (CcO) is a pivotal enzyme of the mitochondrial respiratory chain, which sustains bioenergetics of eukaryotic cells. Cox12, a peripheral subunit of CcO 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 CcO oxidase. In one population, the enhanced bioenergetics was caused by a A375V mutation in the cytosolic 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.

AB - Cytochrome c oxidase (CcO) is a pivotal enzyme of the mitochondrial respiratory chain, which sustains bioenergetics of eukaryotic cells. Cox12, a peripheral subunit of CcO 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 CcO oxidase. In one population, the enhanced bioenergetics was caused by a A375V mutation in the cytosolic 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.

KW - Humans

KW - Prions/genetics

KW - Peptide Termination Factors/metabolism

KW - Saccharomyces cerevisiae Proteins/genetics

KW - Cytochrome-c Oxidase Deficiency

KW - Heat-Shock Proteins/metabolism

KW - Saccharomyces cerevisiae/metabolism

KW - Electron Transport Complex IV/metabolism

UR - https://www.mendeley.com/catalogue/922d7e3f-48f9-399c-81d0-66b335ee34e1/

UR - http://www.scopus.com/inward/record.url?scp=85142403724&partnerID=8YFLogxK

U2 - 10.1091/mbc.E21-10-0499

DO - 10.1091/mbc.E21-10-0499

M3 - Article

C2 - 36129767

VL - 33

SP - ar130

JO - Molecular Biology of the Cell

JF - Molecular Biology of the Cell

SN - 1059-1524

IS - 14

ER -

ID: 99683819