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J Biol Chem, Vol. 275, Issue 20, 15449-15457, May 19, 2000
From the The vacuolar-type H+-ATPase
(V-ATPase) is composed of a peripherally bound (V1) and a
membrane-associated (V0) complex. V1 ATP
hydrolysis is thought to rotate a central stalk, which in turn, is
hypothesized to drive V0 proton translocation. Transduction of torque exerted by the rotating stalk on V0 requires a
fixed structural link (stator) between the complexes to prevent energy loss through futile rotation of V1 relative to
V0; this work sought to identify stator components. The
95-kDa V-ATPase subunit, Vph1p, has a cytosolic NH2
terminus (Nt-Vph1p) and a membrane-associated COOH terminus. Two-hybrid
assays demonstrated that Nt-Vph1p interacts with the catalytic
V1 subunit, Vma1p. Co-immunoprecipitation of Vma1p with
Nt-Vph1p confirmed the interaction. Expression of Nt-Vph1p in a
Evidence That the NH2 Terminus of Vph1p, an Integral
Subunit of the V0 Sector of the Yeast V-ATPase, Interacts
Directly with the Vma1p and Vma13p Subunits of the V1
Sector*
§,,, and¶
Hospital for Sick Children, Toronto, Ontario
M5G 1X8, Canada, the ¶ Faculty of Dentistry, University of
Toronto, Toronto, Ontario M5G 1G6, Canada, and the
§ Department of Medicine, University of Toronto, Toronto,
Ontario M5G 2C4, Canada
vph1 mutant was necessary to recruit Vma13p to
V1. Vma13p bound to Nt-Vph1p in vitro
demonstrating direct interaction. Limited trypsin digests cleaves both
Nt-Vph1p and Vma13p. The same tryptic treatment results in a loss of
proton translocation while not reducing bafilomycin
A1-sensitive ATP hydrolysis. Trypsin cleaved Vph1p at
arginine 53. Elimination of the tryptic cleavage site by substitution
of arginine 53 to serine partially protected vacuolar acidification
from trypsin digestion. These results suggest that Vph1p may function
as a component of a fixed structural link, or stator, coupling
V1 ATP hydrolysis to V0 proton translocation.
*
This work was support by Medical Research Council of Canada
Operating Grant MT12053 and a Medical Research Council of Canada scholarship (to M. F. M.).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.
To whom correspondence should be addressed: Faculty of
Dentistry Research Institute, 124 Edward St., Rm. 430, Faculty of
Dentistry, University of Toronto, Toronto, Ontario M5G 1G6, Canada.
Tel.: 416-979-4900 (ext. 4392); Fax: 416-979-4936; E-mail:
m.manolson@utoronto.ca.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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