High impact information on TFP3

• Mutations at the corresponding sites in the VMA11 and VMA16 genes of S. cerevisiae, which encode the c' and c" subunits, did not confer resistance to the drugs [1].
• Analysis of vmaDelta strains showed that binding of V0 subunits to Vma21p was mediated by the proteolipid subunit Vma11p [2].
• Limited proteolysis experiments with epitope-tagged copies of the proteolipids have revealed that the N and the C termini of c (Vma3p) and c' (Vma11p) were in the lumen of the vacuole [3].
• The VMA11 gene was isolated from a yeast genomic DNA library by complementation of the vma11 mutation [4].
• These cDNAs encoded a protein of unknown function, a component (VMA11) of the vacuolar H(+)-ATPase and a component (cytochrome c oxidase subunit VIa) of the mitochondrial electron transport chain, respectively [5].

Biological context of TFP3

• Cells disrupted for the VMA16 gene displayed the same phenotypes as those lacking either Vma3p or Vma11p; the mutant cells lost V-ATPase activity and failed to assemble V-ATPase subunits onto the vacuolar membrane [6].

Anatomical context of TFP3

• 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 [4].

Other interactions of TFP3

• Surprisingly, loss-of-function mutations of either Vma11p Glu145 or Vma16p Glu108 resulted in a higher degree of assembly of the V1 subunits onto the V0 subcomplex in the vacuolar membrane [6].

Analytical, diagnostic and therapeutic context of TFP3

• Epitope-tagged Vma11p and Vma16p were detected on the vacuolar membrane by immunofluorescence microscopy [6].

References