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

2021 ◽  
Author(s):  
Pawan Kumar Saini ◽  
Hannah Dawitz ◽  
Andreas Aufschnaiter ◽  
Jinsu Thomas ◽  
Amelie Amblard ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Respiratory Chain ◽  
Experimental Evolution ◽  
Mitochondrial Respiratory Chain ◽  
Oxidase Deficiency ◽  
Functional Connection ◽  
Amyloid Aggregates ◽  
Exact Function ◽  
Mitochondrial Respiratory

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.

Carbon Monoxide Specifically Inhibits Cytochrome C Oxidase of Human Mitochondrial Respiratory Chain

2003 ◽  
Vol 93 (3) ◽  
pp. 142-146 ◽  
Author(s):  
Jose-Ramon Alonso ◽  
Francesc Cardellach ◽  
Sònia López ◽  
Jordi Casademont ◽  
Òscar Miró
Keyword(s):  
Carbon Monoxide ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Respiratory Chain ◽  
Mitochondrial Respiratory Chain ◽  
Mitochondrial Respiratory

New perspectives on the assembly process of mitochondrial respiratory chain complex cytochrome c oxidase

Mitochondrion ◽  
2002 ◽  
Vol 2 (1-2) ◽  
pp. 117-128 ◽  
Author(s):  
Cristina Ugalde ◽  
Marieke J.H Coenen ◽  
Murtada H Farhoud ◽  
Stefanie Gilinsky ◽  
Werner J.H Koopman ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Respiratory Chain ◽  
Chain Complex ◽  
Mitochondrial Respiratory Chain ◽  
Assembly Process ◽  
Respiratory Chain Complex ◽  
Mitochondrial Respiratory Chain Complex ◽  
Mitochondrial Respiratory

Assembly of cytochrome c oxidase: what can we learn from patients with cytochrome c oxidase deficiency?

2001 ◽  
Vol 29 (4) ◽  
pp. 446-451 ◽  
Author(s):  
J.-W. Taanman ◽  
S. L. Williams
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Proton Translocation ◽  
Mitochondrial Respiratory Chain ◽  
Site Directed Mutagenesis ◽  
Coupling Mechanism ◽  
Oxidase Deficiency ◽  
Assembly Pathway ◽  
Cytochrome C Oxidase Deficiency ◽  
Prosthetic Groups

Cytochrome c oxidase is an intricate metalloprotein that transfers electrons from cytochrome c to oxygen in the last step of the mitochondrial respiratory chain. It uses the free energy of this reaction to sustain a transmembrane electrochemical gradient of protons. Site-directed mutagenesis studies of bacterial terminal oxidases and the recent availability of refined crystal structures of the enzyme are rapidly expanding the understanding of the coupling mechanism between electron transfer and proton translocation. In contrast, relatively little is known about the assembly pathway of cytochrome c oxidase. Studies in yeast have indicated that assembly is dependent on numerous proteins in addition to the structural subunits and prosthetic groups. Human homologues of a number of these assembly factors have been identified and some are now known to be involved in disease. To dissect the assembly pathway of cytochrome c oxidase, we are characterizing tissues and cell cultures derived from patients with genetically defined cytochrome c oxidase deficiency, using biochemical, biophysical and immunological techniques. These studies have allowed us to identify some of the steps of the assembly process.

Effects of extensively oxidized low-density lipoprotein on mitochondrial function and reactive oxygen species in porcine aortic endothelial cells

2010 ◽  
Vol 298 (1) ◽  
pp. E89-E98 ◽  
Author(s):  
Subir K. Roy Chowdhury ◽  
Ganesh V. Sangle ◽  
Xueping Xie ◽  
Gerald L. Stelmack ◽  
Andrew J. Halayko ◽  
...  
Keyword(s):  
Reactive Oxygen Species ◽  
Cardiovascular Disease ◽  
Enzyme Activity ◽  
Cytochrome C ◽  
Respiratory Chain ◽  
Complex I ◽  
Oxidized Ldl ◽  
Mitochondrial Respiratory Chain ◽  
Oxygen Species ◽  
Mitochondrial Respiratory

Atherosclerotic cardiovascular disease is the leading cause of mortality in the Western world. Dysfunction of the mitochondrial respiratory chain and overproduction of reactive oxygen species (ROS) are associated with atherosclerosis and cardiovascular disease. Oxidation increases the atherogenecity of LDL. Oxidized LDL may be apoptotic or nonapoptotic for vascular endothelial cells (EC), depending on the intensity of oxidation. A previous study demonstrated that nonapoptotic oxidized LDL increased activity of mitochondrial complex I in human umbilical vein EC. The present study examined the impact of extensively oxidized LDL (eoLDL) on oxygen consumption and the activities of key enzymes in the mitochondrial respiratory chain of cultured porcine aortic EC. Oxygraphy detected that eoLDL significantly reduced oxygen consumption in various mitochondrial complexes. Treatment with eoLDL significantly decreased NADH-ubiquinone dehydrogenase (complex I), succinate cytochrome c reductase (complex II/III), ubiquinone cytochrome c reductase (complex III), and cytochrome c oxidase (complex IV) activities and the NAD+-to-NADH ratio in EC compared with mildly oxidized LDL, LDL, or vehicle. Butylated hydroxytoluene, a potent antioxidant, normalized eoLDL-induced reductions in complex I and III enzyme activity in EC. Mitochondria-associated intracellular ROS and release of ROS from EC were significantly increased after eoLDL treatment. These findings suggest that eoLDL impairs enzyme activity in mitochondrial respiratory chain complexes and increases ROS generation from mitochondria of arterial EC. Collectively, these effects could contribute to vascular injury and atherogenesis under conditions of hypercholesterolemia and oxidative stress.

scholarly journals Adaptation of respiratory chain biogenesis to cytochrome c oxidase deficiency caused by SURF1 gene mutations

2012 ◽  
Vol 1822 (7) ◽  
pp. 1114-1124 ◽  
Author(s):  
Nikola Kovářová ◽  
Alena Čížková Vrbacká ◽  
Petr Pecina ◽  
Viktor Stránecký ◽  
Ewa Pronicka ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Respiratory Chain ◽  
Gene Mutations ◽  
Oxidase Deficiency ◽  
Cytochrome C Oxidase Deficiency
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