Mutational Analysis of Subunit G (Vma10p) of the Yeast Vacuolar H+-ATPase
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چکیده
منابع مشابه
Structural organization of the yeast vacuolar H+-ATPase The yeast vacuolar proton-translocating ATPase
The yeast vacuolar proton-translocating ATPase (VATPase) is structurally very similar to the V-ATPases of other fungi, plants and animals (for reviews, see Stevens and Forgac, 1997; Forgac, 1999; Nelson and Harvey, 1999). In all these systems, the V-ATPase is composed of a complex of peripheral membrane proteins containing the ATP binding sites attached to a complex of integral membrane protein...
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trichophyton rubrum is an anthropophilic fungus causing up to 90% of chronic cases of dermatophytosis. several properties of this fungus have been investigated so far. however, a few studies were carried out in the field of molecular biology of this fungus. in the present study, we tried to identify the subunit g of its vacuolar atpase (v-atpase). pairs of 21 nt primers were designed from highl...
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Ac45 is a type I transmembrane protein associated with vacuolar H+-ATPase, a proton pump mediating the acidification of multiple intracellular organelles. In this study, we examined the intracellular routing of Ac45 in transfected CV-1 fibroblasts. Steady state immunolabeling showed that Ac45 is located on the plasma membrane and in a vacuolar compartment in the juxtanuclear region. Antibody in...
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The proton-translocating ATPase (H(+)-ATPase) found on the membrane of the yeast vacuole is the best characterized member of the V-type ATPase family. Biochemical and genetic screens have led to the identification of 14 genes, the majority designated VMA (for vacuolar membrane ATPase) encoding subunits of the enzyme complex. At least eight genes encode for proteins comprising the peripherally a...
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The subunit structure of the vacuolar H(+)-ATPase (V-ATPase) membrane sector is not entirely known. The proteolipid is the only subunit that has been implicated in the mechanism of energy transfer in the enzyme. We have identified a protein (M16) that co-purifies with the V-ATPase complex from bovine chromaffin granules. Information obtained from the amino acid sequence of a proteolytic fragmen...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2000
ISSN: 0021-9258
DOI: 10.1074/jbc.m006640200