Abstract
A cDNA for the GATA-6 (GATA-GT1) DNA binding protein was cloned from a library of the human gastric adenocarcinoma cell line MKN45. The deduced amino acid sequence (449 residues) indicates that the primary structure of human GATA-6 is highly homologous to that of the rat protein. The potential phosphorylation site for protein kinases (A and C), and histidine and alanine clusters are conserved. Whereas the rat H +/K +-ATPase α and β subunit genes have two and three GATA protein binding sites in their promoter regions, respectively, the human α subunit gene has only one binding site [Maeda, M., Kubo, K., Nishi, T. and Futai, M. (1996) J. Exp. Biol. 199, 513–520]. We cloned the 5′-upstream region of the human H +/K +-ATPase β subunit gene by genome walking and found that it also has a single GATA protein binding site near the TATA ☐. The GATA sites of the human α and β subunit genes are recognized by the zinc finger domain of human GATA-6. The conservation of the GATA protein binding sites suggests that they are important for the gene regulation of the human and rat H +/K +-ATPase.
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