Partial assembly of the yeast mitochondrial ATP synthase.

The mitochondrial ATP synthase is a molecular motor that drives the phosphorylation of ADP to ATP. The yeast mitochondrial ATP synthase is composed of at least 19 different peptides, which comprise the F1 catalytic domain, the F0 proton pore, and two stalks, one of which is thought to act as a stator to link and hold F1 to F0, and the other as a rotor. Genetic studies using yeast Saccharomyces cerevisiae have suggested the hypothesis that the yeast mitochondrial ATP synthase can be assembled in the absence of 1, and even 2, of the polypeptides that are thought to comprise the rotor. However, the enzyme complex assembled in the absence of the rotor is thought to be uncoupled, allowing protons to freely flow through F0 into the mitochondrial matrix. Left uncontrolled, this is a lethal process and the cell must eliminate this leak if it is to survive. In yeast, the cell is thought to lose or delete its mitochondrial DNA (the petite mutation) thereby eliminating the genes encoding essential components of F0. Recent biochemical studies in yeast, and prior studies in E. coli, have provided support for the assembly of a partial ATP synthase in which the ATP synthase is no longer coupled to proton translocation.