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Originally published In Press as doi:10.1074/jbc.M006640200 on August 31, 2000

J. Biol. Chem., Vol. 275, Issue 47, 37232-37239, November 24, 2000
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Mutational Analysis of Subunit G (Vma10p) of the Yeast Vacuolar H+-ATPase*

Colleen M. H. Charsky, Nicole J. Schumann, and Patricia M. KaneDagger

From the Department of Biochemistry and Molecular Biology, State University of New York, Upstate Medical University, Syracuse, New York 13210

The G subunit of V-ATPases is a soluble subunit that shows homology with the b subunit of F-ATPases and may be part of the "stator" stalk connecting the peripheral V1 and membrane V0 sectors. When the N-terminal half of the G subunit is modeled as an alpha  helix, most of the conserved residues fall on one face of the helix (Hunt, I. E., and Bowman, B. J. (1997) J. Bioenerg. Biomembr. 29, 533-540). We probed the function of this region by site-directed mutagenesis of the yeast VMA10 gene. Stable G subunits were produced in the presence of Y46A and K55A mutations, but subunit E was destabilized, resulting in loss of the V-ATPase assembly. Mutations E14A and K50A allowed wild-type growth and assembly of V-ATPase complexes, but the complexes formed were unstable. Mutations R25A and R25L stabilized V-ATPase complexes relative to wild-type and partially inhibited disassembly of V1 from V0 in response to glucose deprivation even though the mutant enzymes were fully active. A 2-amino acid deletion in the middle of the predicted N-terminal helix (Delta Q29D30) allowed assembly of a functional V-ATPase. The results indicate that, although the N-terminal half of the G subunit is essential for V-ATPase activity, either this region is not a rigid helix or the presence of a continuous, conserved face of the helix is not essential.

* This work was supported in part by National Institutes of Health Grant R01-GM50322 (to P. M. K.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger An American Heart Association Established Investigator. To whom correspondence should be addressed: Dept. of Biochemistry and Molecular Biology, State University of New York, Upstate Medical University, 750 E. Adams St., Syracuse, NY 13210. Tel.: 315-464-8742; Fax: 315-464-8736; E-mail: kanepm@mail.upstate.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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