Disease relevance of VMA5

• Vma5p (subunit C) of the yeast V-ATPase was produced in Escherichia coli and purified to homogeneity [1].

High impact information on VMA5

• Furthermore, a chimeric yeast V-ATPase with mouse the C2-a or C2-b isoform showed a lower Km(ATP) and lower proton transport activity than that with C1 or Vma5p (yeast C subunit) [2].
• High level overexpression of Vma5p and Vma13p was lethal even in wild-type cells [3].
• Cells overexpressing Vma5p and Vma13p demonstrate a classic Vma(-) growth phenotype [3].
• We report here the characterization of two genes, VMA4 and VMA5, that encode peripheral subunits of the vacuolar H(+)-ATPase [4].
• Representatives in five complementation groups were identified, including four novel mutant vma5, vma21, vma22, and vma23, all of which were defective in vacuolar ATPase enzyme activity [4].

Biological context of VMA5

• The expressed protein consists of 412 residues: 392 from the reading frame of Vma5p and 20 N-terminal residues originating from the plasmid [5].

Anatomical context of VMA5

• A cdc24-4ls delta vma5::LEU2 double mutant did not exhibit synthetic lethality, suggesting that the csl5/vma5 cdc24-4ls synthetic-lethality was not simply due to altered vacuole function [6].

Associations of VMA5 with chemical compounds

• Subunit C of the vacuolar-type ATPase from the vanadium-rich ascidian Ascidia sydneiensis samea rescued the pH sensitivity of yeast vma5 mutants [7].

Other interactions of VMA5

• Defined sites of interaction between subunits E (Vma4p), C (Vma5p), and G (Vma10p) within the stator structure of the vacuolar H+-ATPase [8].

Analytical, diagnostic and therapeutic context of VMA5

• To elucidate subunit C function, we performed random and site-directed mutagenesis of the yeast VMA5 gene [9].
• Analysis of secondary structure by circular dichroism spectroscopy showed that Vma5p comprises 64% alpha-helix and 17% beta-sheet content [1].
• Localization of subunit C (Vma5p) in the yeast vacuolar ATPase by immuno electron microscopy [10].
• The expression, crystallization and phasing of subunit C (Vma5p) of the yeast (Saccharomyces cerevisiae) vacuolar proton-translocating ATPase (V-ATPase) is described [5].
• Projection maps of a V(1)-Vma5p hybrid complex, composed of subunit C (Vma5p) of Saccharomyces cerevisiae V-ATPase and the C-depleted V(1) from Manduca sexta, were determined from single particle electron microscopy [11].

References