Interaction between subunit C (Vma5p) of the yeast vacuolar ATPase and the stalk of the C-depleted V(1) ATPase from Manduca sexta midgut.

Biochim Biophys Acta

Department of Biophysical Chemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, Netherlands.

Published: June 2005

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. V(1)-Vma5p consists of a headpiece and an elongated wedgelike stalk with a 2.1x3.0 nm protuberance and a 9.5x7.5 globular domain, interpreted to include Vma5p. The interaction face of Vma5p in V(1) was explored by chemical modification experiments.

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http://dx.doi.org/10.1016/j.bbabio.2005.02.001DOI Listing

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Department of Biophysical Chemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, Netherlands.

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