Metabolic modulation of transport coupling ratio in yeast plasma membrane H+-ATPase

Abstract

The plasma membrane proton pump (H+-ATPase) of yeast energizes solute uptake by secondary transporters and regulates cytoplasmic pH. The addition of glucose to yeast cells stimulates proton efflux mediated by the H+- ATPase. A >50-fold increase in proton extrusion from yeast cells is observed in vivo, whereas the ATPase activity of purified plasma membranes is increased maximally 8-fold after glucose treatment (Serrano, R. (1983) FEBS Lett. 156, 11-14). The low capacity of yeast cells for proton extrusion in the absence of glucose can be explained by the finding that, in H+-ATPase isolated from glucose-starved cells, ATP hydrolysis is essentially uncoupled from proton pumping. The number of protons transported per ATP hydrolyzed is significantly increased after glucose activation. We suggest that intrinsic uncoupling is an important mechanism for regulation of pump activity.