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Volume 272, Number 39, Issue of September 26, 1997 pp. 24387-24392
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Three vha Genes Encode Proteolipids of Caenorhabditis elegans Vacuolar-type ATPase
GENE STRUCTURES AND PREFERENTIAL EXPRESSION IN AN H-SHAPED EXCRETORY CELL AND RECTAL CELLS

(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.

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