In vivo labeling and analysis of mitochondrial translation products in budding and in fission yeasts.

Mitochondrial biogenesis requires the contribution of two genomes and of two compartmentalized protein synthesis systems (nuclear and mitochondrial). Mitochondrial protein synthesis is unique on many respects, including the use of a genetic code with deviations from the universal code, the use of a restricted number of transfer RNAs, and because of the large number of nuclear encoded factors involved in assembly of the mitochondrial biosynthetic apparatus. The mitochondrial biosynthetic apparatus is involved in the actual synthesis of a handful of proteins encoded in the mitochondrial DNA.

Suppression mechanisms of COX assembly defects in yeast and human: insights into the COX assembly process.

Eukaryotic cytochrome c oxidase (COX) is the terminal enzyme of the mitochondrial respiratory chain. COX is a multimeric enzyme formed by subunits of dual genetic origin whose assembly is intricate and highly regulated. In addition to the structural subunits, a large number of accessory factors are required to build the holoenzyme.

Physiological oxygenation status is required for fully differentiated phenotype in kidney cortex proximal tubules.

Hypoxia has been suspected to trigger transdifferentiation of renal tubular cells into myofibroblasts in an epithelial-to-mesenchymal transition (EMT) process. To determine the functional networks potentially altered by hypoxia, rat renal tubule suspensions were incubated under three conditions of oxygenation ranging from normoxia (lactate uptake) to severe hypoxia (lactate production). Transcriptome changes after 4 h were analyzed on a high scale by restriction fragment differential display.