Molecular Cloning of cDNAs Encoding the Proteolipid Subunit of the Vacuolar H<sup>+</sup>-ATPase of Acetabularia acetabulum
2002
M. Habibur Rahman | Mikiko Ikeda
Three cDNAs (named pVC1, pVC2 and pVC3) have been isolated from a giant alga, Acetabularia acetabulum that encoded the N, N´- icyclohexylcarbodimide-binding 16 kDa proteolipid subunit of V-ATPase. The open reading frames of pVC1, pVC2 and pVC3 predicted the polypeptides of 164, 167 and 168 amino acids with the molecular masses of 16.5, 16.7 and 16.8 kDa, respectively. Seventy nine percent identity between pVC1 and pVC2 or pVC3 and 95% identity between pVC2 and pVC3 was observed. PVC1 and pVC2/pVC3 showed extensive divergences in their 3´ -untranslated region, while pVC2 and pVC3 possessed the same 3´ -untranslated region. The deduced amino acid sequences of the three cDNA clones showed extensive similarities with that of proteolipids of oat (75 to 80%), bovine (55%) and yeast (55%) V-ATPase. Based on hydropathy plot, four membrane-spanning domains were predicted, in which domain IV was especially conserved among different species. This domain showed 96-100% identity in amino acid sequences between the A. acetabulum and the oat proteolipid in which a glutamate residue is included, the putative N, N´-dicyclohexylcarbodimide-binding residue.
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