Interaction between subunit C (Vma5p) of the yeast vacuolar ATPase and the stalk of the C-depleted V1 ATPase from Manduca sexta midgut |
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Authors: | Yuriy L. Chaban Egbert J. Boekema |
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Affiliation: | a Department of Biophysical Chemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, Netherlands b Universität des Saarlandes, Fachrichtung 2.5 - Biophysik, D-66421 Homburg, Germany |
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Abstract: | Projection maps of a V1-Vma5p hybrid complex, composed of subunit C (Vma5p) of Saccharomyces cerevisiae V-ATPase and the C-depleted V1 from Manduca sexta, were determined from single particle electron microscopy. V1-Vma5p consists of a headpiece and an elongated wedgelike stalk with a 2.1×3.0 nm protuberance and a 9.5×7.5 globular domain, interpreted to include Vma5p. The interaction face of Vma5p in V1 was explored by chemical modification experiments. |
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Keywords: | V-ATPase V1VO ATPase V1 ATPase Vma5p Reversible disassembly Electron microscopy Manduca sexta Saccharomyces cerevisiae |
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