The yeast vacuole is a primary storage compartment, which also serves as a degradative organelle like the animal cell lysosome. The lumen of the vacuole is acidified by the vacuolar membrane H
+-ATPase, the best-known member of the V-type ATPases of eukaryotic cells. This H
+-ATPase is a multisubunit enzyme consisting of at least eight polypeptides with apparent molecular masses of 100, 69, 60, 42, 36, 32, 27, and 17, kDa. The genes (
VMA) for seven of these subunits have been isolated, and their deletions have been constructed. These
uma deletion mutants were defective in vacuolar acidification and showed common growth phenotypes : sensitive to pH and Ca
2+ in the medium and deficient in respiration (Pet
-). The screening for yeast calcium-sensitive mutants (
cls) that are also Pet
-have identified three novel genes,
VMA 11-VMA 13. VMA 11 and VMA 13 encode putative subunits of the vacuolar membrane H
+-ATPase. The
VMA 12 gene product is not included in the enzyme but is required for the assembly and/or targeting of the enzyme.
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