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Analysis of Mitochondrial Protein Synthesis: De Novo Translation, Steady-State Levels, and Assembled OXPHOS Complexes.

Hilander, T; Konovalova, S; Terzioglu, M; Tyynismaa, H (2018) Analysis of Mitochondrial Protein Synthesis: De Novo Translation, Steady-State Levels, and Assembled OXPHOS Complexes. Curr Protoc Toxicol, 77 (1). e56. ISSN 1934-9262 https://doi.org/10.1002/cptx.56
SGUL Authors: Hilander, Taru

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Abstract

Mitochondria are multifunctional organelles with their own genome and protein synthesis machinery. The 13 proteins encoded by mitochondrial DNA (mtDNA) are core subunits of the oxidative phosphorylation (OXPHOS) system producing the majority of cellular ATP. Yet most mitochondrial proteins are encoded by nuclear genes, synthesized by cytosolic ribosomes, and imported into mitochondria. Therefore, disturbances in cytosolic proteostasis have consequences on the gene expression and synthesis of mtDNA-encoded proteins and overall on mitochondrial function. Internal and environmental factors such as mutations, aging, oxidative stress, and toxic agents can affect the translation and the stability of mitochondrial proteins and lead to OXPHOS dysfunction. Here, methods for analysis of mitochondrial translation rate and protein stability using radioactive and non-radioactive technique as well as the methods for studying steady-state levels and assembly of OXPHOS complexes are described. © 2018 by John Wiley & Sons, Inc.

Item Type: Article
Additional Information: This is the peer reviewed version of the following article: Hilander, T., Konovalova, S., Terzioglu, M., & Tyynismaa, H. (2018). Analysis of mitochondrial protein synthesis: De novo translation, steady‐state levels, and assembled OXPHOS complexes. Current Protocols in Toxicology, 77, e56., which has been published in final form at https://doi.org/10.1002/cptx.56. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Use of Self-Archived Versions.
Keywords: OXPHOS complexes, mitochondria, protein synthesis, proteostasis
SGUL Research Institute / Research Centre: Academic Structure > Molecular and Clinical Sciences Research Institute (MCS)
Journal or Publication Title: Curr Protoc Toxicol
ISSN: 1934-9262
Language: eng
Dates:
DateEvent
17 August 2018Published
31 July 2018Published Online
25 April 2018Accepted
Publisher License: Publisher's own licence
PubMed ID: 30063298
Go to PubMed abstract
URI: http://sgultest.da.ulcc.ac.uk/id/eprint/110069
Publisher's version: https://doi.org/10.1002/cptx.56

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