Biolayer interferometry of lipid nanodisc-reconstituted yeast vacuolar H+-ATPase

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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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Composition and assembly of the yeast vacuolar H(+)-ATPase complex.

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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Renal vacuolar H+-ATPase.

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Structure of the yeast vacuolar ATPase.

The subunit architecture of the yeast vacuolar ATPase (V-ATPase) was analyzed by single particle transmission electron microscopy and electrospray ionization (ESI) tandem mass spectrometry. A three-dimensional model of the intact V-ATPase was calculated from two-dimensional projections of the complex at a resolution of 25 angstroms. Images of yeast V-ATPase decorated with monoclonal antibodies ...

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Regulation and reversibility of vacuolar H(+)-ATPase.

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ژورنال

عنوان ژورنال: Protein Science

سال: 2017

ISSN: 0961-8368

DOI: 10.1002/pro.3143