VMA11, a novel gene that encodes a putative proteolipid, is indispensable for expression of yeast vacuolar membrane H(+)-ATPase activity.

A gene, VMA11, is indispensable for expression of the vacuolar membrane H(+)-ATPase activity in the yeast Saccharomyces cerevisiae (Ohya, Y., Umemoto, N., Tanida, I., Ohta, A., Iida, H., and Anraku, Y. (1991) J. Biol. Chem. 266, 13971-13977). The VMA11 gene was isolated from a yeast genomic DNA library by complementation of the vma11 mutation. The nucleotide sequence of the gene predicts a hydrophobic proteolipid of 164 amino acids with a calculated molecular mass of 17,037 daltons. The deduced amino acid sequence shows 56.7% identity, and significant coincidence in amino acid composition with the 16-kDa subunit c (a VMA3 gene product) of the yeast vacuolar membrane H(+)-ATPase. VMA11 and VMA3 on a multicopy plasmid did not suppress the vma3 and vma11 mutation, respectively, suggesting functional independence of the two gene products. Biochemical detection of the VMA11 gene product was unsuccessful, but vacuoles in the VMA11-disrupted cells were not assembled with either subunit c or subunits a and b of the H(+)-ATPase, resulting in defects of the activity and in vivo vacuolar acidification.