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J. Biol. Chem., Vol. 269, Issue 42, 25974-25977, Oct, 1994
LA Graham, KJ Hill and TH Stevens
The Saccharomyces cerevisiae vacuolar proton-translocating ATPase (V-
ATPase) is composed of at least 10 subunits belonging to either the
peripheral V1 or integral membrane V0 subcomplex. We have characterized a
novel 14-kDa V-ATPase subunit (Vma7p), encoded by the VMA7 gene, which
exhibits features common to both V1 and V0 subunit proteins. Vma7p is a
hydrophilic protein of 118 amino acids with a predicted molecular mass of
13,452 Da. Vacuolar membranes isolated from a vma7 delta null mutant
contained no V-ATPase activity. Western analysis of vma7 delta cells
revealed greatly reduced levels of the remaining V0 complex V-ATPase
subunits, but normal levels of the V1 subunits. However, the V1 subunits
failed to associate with the vacuolar membrane. Unlike the integral
membrane subunits of the V0 complex, Vma7p was easily stripped from
vacuolar membranes. Density gradient fractionation revealed that Vma7p
associated only with the fully assembled V-ATPase and did not associate
with a separate lower density V0 subcomplex fraction. The unique properties
of the Vma7p may reflect a critical role in stabilizing the V0 complex and
bridging the V1 and V0 complexes to form a functional V-ATPase complex.
VMA7 encodes a novel 14-kDa subunit of the Saccharomyces cerevisiae vacuolar H(+)-ATPase complex
Institute of Molecular Biology, University of Oregon, Eugene 97403.
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