Biosynthesis of the Yeast Mitochondrial H+-ATPase Complex
The elucidation of the mechanism of assembly of multimeric enzyme complexes of the mitochondrial inner membrane is a major challenge in biochemistry. One of these enzyme complexes, the mitochondrial H+-translocating ATPase, has been the focus of intensive investigations in recent years. This enzyme complex, which is the terminal enzyme in oxidative phosphorylation catalyzing in vivo the synthesis of ATP when coupled to the mitochondrial electron transport chain, is assembled from subunits which are synthesized in the mitochondria as well as subunits imported from the extramitochondrial cytoplasm. The formation of the H+-ATPase, therefore, is a complicated process involving the synthesis of its individual subunits on the cytoplasmic and mitochondrial ribosomes, the transport of the cytoplasmically synthesized subunits onto and across the mitochondrial membranes, and the assembly of these subunits into a functional H+-ATPase.
KeywordsEnzyme Complex ATPase Subunit Yeast Mitochondrion Mitochondrial Protein Synthesis Mitochondrial ATPase
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