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(Received for publication, May 13, 1997, and in revised form, July 7, 1997)
From the Department of Molecular Cell Biology, Division of
Biological Science, Institute of Scientific and Industrial
Research, Osaka University, Osaka 567, Japan
The proteolipids of the vacuolar-type
H+-ATPase (V-ATPase) are major components of the
integral membrane sector. The vha-1 and vha-2
(vacuolar-type
H+-ATPase) genes in
Caenorhabditis elegans encode putative 16-kDa proteolipids
and are tandemly localized on chromosome III. The vha-2
gene has three exons, whereas vha-1 has no introns. The deduced amino acid sequences of the two genes exhibit about 60% identity with the homologues from yeast, mouse, and cow. The mRNAs of both vha genes are trans-spliced to spliced
leaders, suggesting that these genes constitute a polycistronic
transcriptional unit. The vha-4 gene consists of four exons
and is very similar to the yeast VMA16 gene that codes for
the 23-kDa proteolipid. This is the first example of three distinct
V-ATPase proteolipids being identified in higher eukaryotes. Northern
blot and transgenic analyses show that the three vha genes
may be highly expressed in the H-shaped excretory cell, rectum, and a
pair of cells posterior to the anus. These results suggest that the
V-ATPase activity may be important for exporting toxic compounds or
metabolic wastes in this organism.
Volume 272, Number 39,
Issue of September 26, 1997
pp. 24387-24392
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
GENE STRUCTURES AND PREFERENTIAL EXPRESSION IN AN H-SHAPED
EXCRETORY CELL AND RECTAL CELLS
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