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(Received for publication, July 23, 1996, and in revised form, November 5, 1996)
From the The vacuolar membrane
H+-ATPase (V-ATPase) of the yeast Saccharomyces
cerevisiae is composed of peripheral catalytic (V1)
and integral membrane (V0) domains. The 17-kDa proteolipid
subunit (VMA3 gene product; Vma3p) is predicted to
constitute at least part of the proton translocating pore of
V0. Recently, two VMA3 homologues,
VMA11 and VMA16 (PPA1), have been
identified in yeast, and VMA11 has been shown to be
required for the V-ATPase activity. Cells disrupted for the
VMA16 gene displayed the same phenotypes as those lacking
either Vma3p or Vma11p; the mutant cells lost V-ATPase activity and
failed to assemble V-ATPase subunits onto the vacuolar membrane.
Epitope-tagged Vma11p and Vma16p were detected on the vacuolar membrane
by immunofluorescence microscopy. Density gradient fractionation
of the solubilized vacuolar proteins demonstrated that the tagged
proteins copurified with the V-ATPase complex. We conclude that Vma11p
and Vma16p are essential subunits of the V-ATPase. Vma3p contains a
conserved glutamic acid residue (Glu137) whose carboxyl
side chain is predicted to be important for proton transport activity.
Mutational analysis of Vma11p and Vma16p revealed that both proteins
contain a glutamic acid residue (Vma11p Glu145 and Vma16p
Glu108) functionally similar to Vma3p Glu137.
These residues could only be functionally substituted by an aspartic
acid residue, because other mutations we examined inactivated the
enzyme activity. Assembly and vacuolar targeting of the enzyme complex
was not inhibited by these mutations. These results suggest that the
three proteolipid subunits have similar but not redundant functions,
each of which is most likely involved in proton transport activity of
the enzyme complex. Yeast cells contain V0 and
V1 subcomplexes in the vacuolar membrane and in the
cytosol, respectively, that can be assembled into the active
V0V1 complex in vivo. Surprisingly, loss-of-function mutations of either Vma11p Glu145 or
Vma16p Glu108 resulted in a higher degree of assembly of
the V1 subunits onto the V0 subcomplex in the
vacuolar membrane.
Volume 272, Number 8,
Issue of February 21, 1997
pp. 4795-4803
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
,
,
Institute of Physical and Chemical Research
(RIKEN), Hirosawa, Wako-shi, Saitama 351-01, Japan, the
§ Institute of Molecular Biology, University of Oregon,
Eugene, Oregon 97403-1229, and the ¶ Department of Biological
Sciences, Graduate School of Science, University of Tokyo, Hongo,
Bunkyo-ku, Tokyo 113, Japan
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T. Nishi, S. Kawasaki-Nishi, and M. Forgac Expression and Localization of the Mouse Homologue of the Yeast V-ATPase 21-kDa Subunit c'' (Vma16p) J. Biol. Chem., August 31, 2001; 276(36): 34122 - 34130. [Abstract] [Full Text] [PDF]
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K. Keenan Curtis and P. M. Kane Novel Vacuolar H+-ATPase Complexes Resulting from Overproduction of Vma5p and Vma13p J. Biol. Chem., January 18, 2002; 277(4): 2716 - 2724. [Abstract] [Full Text] [PDF]
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Y. Arata, J. D. Baleja, and M. Forgac Cysteine-directed Cross-linking to Subunit B Suggests That Subunit E Forms Part of the Peripheral Stalk of the Vacuolar H+-ATPase J. Biol. Chem., January 25, 2002; 277(5): 3357 - 3363. [Abstract] [Full Text] [PDF]
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S. Kawasaki-Nishi, T. Nishi, and M. Forgac Arg-735 of the 100-kDa subunit a of the yeast V-ATPase is essential for proton translocation PNAS, October 23, 2001; 98(22): 12397 - 12402. [Abstract] [Full Text] [PDF]
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