The yeast plasma membrane H+-ATPase generates a membrane electrochemic
al gradient which is required for the secondary uptake of nutrients. A
lthough the ATPase has previously been shown to be post-translationall
y regulated in response to the availability of glucose, there has been
no evidence to date for transcriptional regulation of the ATPase gene
(PMA1). In this work, we have examined the pool of newly synthesized
ATPase that accumulates in secretory vesicles en route to the cell sur
face in the temperature-sensitive secretory mutant sec6-4, and have ob
served changes in the level of ATPase polypeptide as a function of the
glucose concentration in the growth medium. In parallel, there were r
apid and reversible changes in the levels of ATPase mRNA. Finally, whe
n cells were grown on a variety of carbon sources, the amount of ATPas
e polypeptide was proportional to the specific growth rate, suggesting
that PMA1 expression is adjusted according to the metabolic state of
the cell. These results complement the findings of Capieaux et al. (Ca
pieaux, E., Vignais, M.-L., Sentenac, A. and Goffeau, A. (1989). J. Bi
ol. Chem. 264, 7437-7446), who show that the transcriptional factor TU
F/RAP1 binds to upstream activating sequences in the PMA1 gene. Taken
together, the results suggest a model in which transcriptional regulat
ion of the ATPase gene by glucose is mediated by TUF/RAP1.