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J Biol Chem, Vol. 273, Issue 35, 22570-22576, August 28, 1998
From the Division of Biological Sciences, Institute of Scientific
and Industrial Research, Osaka University, CREST of the Japan Science
and Technology Corporation, Osaka 567-0047, Japan
In the vacuolar-type H+-ATPase
(V-ATPase), highly hydrophobic subunits known as the proteolipids are
components of the integral membrane V0 sector. Previously,
we described the identification of three different proteolipid genes in
Caenorhabditis elegans (Oka, T., Yamamoto, R., and Futai,
M. (1997) J. Biol. Chem. 272, 24387-24392):
vha-1 and vha-2 encoded 16-kDa subunits, and
vha-4, a 23-kDa isoform. We report here that a third 16-kDa
gene, vha-3, has been identified on chromosome IV. This is
the first example in which four proteolipid genes have been found in a
single organism. vha-2 and vha-3 exhibited 85%
nucleotide identity within the open reading frames which encoded the
identical amino acid sequence. Northern blot analysis indicated that
all four genes were expressed in a similar pattern during the worm life
cycle; however, studies with transgenic worms indicated that the
vha-3 gene was expressed differently from other proteolipid
genes in a cell-specific manner. These results implied that the
isoforms of the proteolipids may be related to functional differences
of V-ATPases in various cell types.
Another new gene, vha-11, contained seven exons and was
found to be located immediately downstream of vha-3. The
two genes constitute a single transcriptional unit. The VHA-11 protein
had 384 amino acids and shared strong sequence similarities with the C subunit, a component of the peripheral V1
sector of the V-ATPase, from yeast, bovine, and human. Expression of
the vha-11 cDNA complemented a null mutation of
VMA5, the yeast C subunit gene, thus
demonstrating that vha-11 was the functional C
subunit of C. elegans.
Multiple Genes for Vacuolar-type ATPase Proteolipids in
Caenorhabditis elegans
A NEW GENE, vha-3, HAS A DISTINCT CELL-SPECIFIC
DISTRIBUTION
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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