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1 Neurology, University of Miami, Miami, Florida, United States
2 Biochemistry, University of Miami, Miami, Florida, United States
3 Neurology, University of Miami, Miami, Florida, United States; Biochemistry, University of Miami, Miami, Florida, United States
* To whom correspondence should be addressed. E-mail: abarrientos{at}med.miami.edu.
Cytochrome c oxidase (COX), the terminal enzyme of the mitochondrial respiratory chain plays a key role in the regulation of aerobic production of energy. Biogenesis of eukaryotic COX, involves the coordinated action of two genomes. Three mitochondrial DNA encoded subunits form the catalytic core of the enzyme, which contains metal prosthetic groups. Another ten subunits encoded in the nuclear DNA act as a protective shield surrounding the core. COX biogenesis requires the assistance of more than 20 additional nuclear encoded factors acting at all the levels of the process. Expression of the mitochondrial encoded subunits, expression and import of the nuclear encoded subunits, insertion of the structural subunits into the mitochondrial inner membrane, addition of prosthetic groups, assembly of the holoenzyme, further maturation to form a dimer or additional assembly into supercomplexes are all tightly regulated processes in a nuclear-mitochondrial coordinated fashion. Such a regulation ensures the building a highly efficient machine able to catalyze the safe transfer of electrons from cytochrome c to molecular oxygen and ultimately facilitate the aerobic production of ATP. In this review we will focus on describing and analyzing the current knowledge about the different regulatory checkpoints in COX assembly, and the dynamic relationships between the different factors involved in the process. We have used information mostly obtained from the suitable yeast model, but also from bacterial and animal systems, by means of large-scale genetic, molecular biology and physiological approaches and by integrating information concerning individual elements into a cellular system network.
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