Showing papers on "ATP transport published in 1978"

The Biosynthesis of the Mitochondria1 ADP, ATP Translocator

Abstract: Studies of adenine nucleotide transport across the inner mitochondrial membrane suggested that a specific membrane protein serves as the carrier of ADP and ATP [l]. The sites of these components were defined first by binding studies with ADP and ATP [2] and then using the more tightly binding inhibitors atractylate, carboxyatractylate and bongkrekate [3 - 51. On this basis the membrane protein responsible for the ADP,ATP transport was first isolated from beef heart mitochondria as a carboxyatractylatebinding protein and found to be the most abundant polypeptide of mitochondria [6,7]. More recently, the bongkrekate complex was also isolated and found to contain the identical protein as the carboxyatractylate complex [8]. This translocator protein must be expected to be present in all mitochondria because of its fundamental role in the function of the mitochondria. The biogenesis of this very hydrophobic membrane protein is therefore of great interest also for the problem of the biogenesis and origin .of mitochondria. The biogenesis of the ADP,ATP carrier was discussed previously based on studies of the adenine nucleotide transport in mitochondria from yeast mutants [14-231. For instance, it was claimed that mutants resistant to bongkrekate exist, and furthermore that the adenine nucleotide translocation was changed by inhibitors of mitochondrial protein synthesis [18,19]. However, no general consensus was reached. All these studies did not deal directly with the biogenesis of the translocator protein since the corresponding membrane component was not yet identified. For studying the biogenesis of the ADP,ATP carrier directly, the carboxyatractylate-protein complex has