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J. Biol. Chem., Vol. 276, Issue 21, 17941-17948, May 25, 2001
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From the Department of Physiology, Tufts University School of
Medicine, Boston, Massachusetts 02111
The 100 kDa a-subunit of the yeast vacuolar
(H+)-ATPase (V-ATPase) is encoded by two genes,
VPH1 and STV1. These genes encode unique
isoforms of the a-subunit that have previously been shown to reside in
different intracellular compartments in yeast. Vph1p localizes to the
central vacuole, whereas Stv1p is present in some other compartment,
possibly the Golgi or endosomes. To compare the properties of V-ATPases
containing Vph1p or Stv1p, Stv1p was expressed at higher than normal
levels in a strain disrupted in both genes, under which conditions
V-ATPase complexes containing Stv1p appear in the vacuole. Complexes
containing Stv1p showed lower assembly with the peripheral
V1 domain than did complexes containing Vph1p. When
corrected for this lower degree of assembly, however, V-ATPase
complexes containing Vph1p and Stv1p had similar kinetic properties.
Both exhibited a Km for ATP of about 250 µM, and both showed resistance to sodium azide and
vanadate and sensitivity to nanomolar concentrations of concanamycin A. Stv1p-containing complexes, however, showed a 4-5-fold lower ratio of
proton transport to ATP hydrolysis than Vph1p-containing complexes. We
also compared the ability of V-ATPase complexes containing Vph1p or
Stv1p to undergo in vivo dissociation in response to glucose depletion. Vph1p-containing complexes present in the vacuole showed dissociation in response to glucose depletion, whereas Stv1p-containing complexes present in their normal intracellular location (Golgi/endosomes) did not. Upon overexpression of Stv1p, Stv1p-containing complexes present in the vacuole showed
glucose-dependent dissociation. Blocking delivery of
Vph1p-containing complexes to the vacuole in vps21
Yeast V-ATPase Complexes Containing Different Isoforms of the
100-kDa a-subunit Differ in Coupling Efficiency and in Vivo
Dissociation*
,, and
and
vps27 strains caused partial inhibition of
glucose-dependent dissociation. These results suggest that dissociation of the V-ATPase complex in vivo is controlled
both by the cellular environment and by the 100-kDa a-subunit isoform present in the complex.
*
This work was supported by National Institutes of Health
Grant GM34478 (to M. F.) and a Charles A. King Trust Fellowship Award (to T. N.).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.
These authors contributed equally to this work.
§
To whom correspondence should be addressed: Dept. of Physiology,
Tufts University School of Medicine, 136 Harrison Ave., Boston, MA
02111. Tel.: 617-636-6939; Fax: 617-636-0445; E-mail address: michael.forgac@tufts.edu.
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