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VMA13
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Abstract
Mutant phenotypes associated with vma13 cells are identical to those found for vma2 mutants (see VMA2 entry p. 261)1,3_ However, deletion of the VMA13 gene in yeast results in strains that are deficient for vacuolar acidification12. The remaining vacuolar H+-ATPase subunits (Vma1p, Vma2p, Vma3p, Vma4p, Vma5p, and Vph 1p) continue to associate with the vacuolar membrane in the absence of Vma13p. This is surprising given that several of the remaining subunits, including the Vma1, Vma2, Vma4, and Vma5 polypeptides, are hydrophilic proteins that are thought to peripherally associate with the vacuolar membrane only when the H+-ATPase is fully assembled45. These results suggest that although Vma13p is essential for the activity of the vacuolar W-ATPase, it is not required for some level of enzyme assembly onto the vacuolar membrane.
Title: VMA13
Description:
Abstract
Mutant phenotypes associated with vma13 cells are identical to those found for vma2 mutants (see VMA2 entry p.
261)1,3_ However, deletion of the VMA13 gene in yeast results in strains that are deficient for vacuolar acidification12.
The remaining vacuolar H+-ATPase subunits (Vma1p, Vma2p, Vma3p, Vma4p, Vma5p, and Vph 1p) continue to associate with the vacuolar membrane in the absence of Vma13p.
This is surprising given that several of the remaining subunits, including the Vma1, Vma2, Vma4, and Vma5 polypeptides, are hydrophilic proteins that are thought to peripherally associate with the vacuolar membrane only when the H+-ATPase is fully assembled45.
These results suggest that although Vma13p is essential for the activity of the vacuolar W-ATPase, it is not required for some level of enzyme assembly onto the vacuolar membrane.