Abstract
We obtained a cDNA clone(PP10) for the vacuolar membrane proton-translocating inorganic pyrophosphatase from barley roots by immunoscreening. The nucleotide sequence contained a 2308 bp open reading frame capable of coding for a polypeptide with 761 amino acids(Mr79,841). The polypeptide is highly hydrophobic and 12 membrane-spanning regions are deduced from the hydropathic evaluation. The characteristic cluster of the basic and acidic residues is observed in the hydrophilic segment. A consensus sequence with the dicyclohexylcarbodiimide binding subunits of F OF 1-type and vacuolar-type H +-ATPase is also observed in the membrane-spanning domain 5. Comparison of the deduced amino acid sequence with that of pyrophosphatase cDNA from Arabidopsis thaliana revealed 85.8% homology.
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