Structure and Function of the Subunits of the Vacuolar Membrane H + -ATPase of Saccharomyces Cerevisiae

We have found a novel H+-translocating ATPase in vacuolar membranes of the yeast Saccharomyces cerevisiae (Kakinuma et al., 1981; Uchida et al., 1985). Using a preparation of right-side-out vacuolar membrane vesicles of high purity (Ohsumi and Anraku, 1981), we showed that the H+-ATPase generates an electrochemical potential difference of protons across the membrane of 180 mV, interior acid (Kakinuma et al., 1981), and that the enzyme serves as a common energy-donating system for seven n H+/amino-acid antiport systems and one H+/Ca2+ antiport, which all are present in the vacuolar membrane (Sato et al., 1984; Ohsumi and Anraku, 1983; Anraku, 1987).