Analysis of Mitochondrial Protein Synthesis: De Novo Translation, Steady‐State Levels, and Assembled OXPHOS Complexes. Issue 1 (31st July 2018)

• Record Type: Journal Article
• Authors: Hilander, Taru; Konovalova, Svetlana; Terzioglu, Mügen; Tyynismaa, Henna
• Editors: Bus, James S.; Costa, Lucio G.; Hodgson, Ernest; Lawrence, David A.; Reed, Donald J.
• Is Part Of: Current protocols in toxicology. Volume 77:Issue 1(2018)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2018-07-31
• Subjects: mitochondria -- protein synthesis -- proteostasis -- OXPHOS complexes; Toxicology -- Laboratory manuals; Toxicology -- methods; Toxicology; Laboratory Manual; Electronic books; Laboratory manuals; 571.95028
• DOI: 10.1002/cptx.56
• Languages: English
• ISSNs: 1934-9254

Abstract

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.