Molecular cloning of cDNA for vacuolar membrane proton-translocating inorganic pyrophosphatase in Hordeum vulgare.
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 (M(r) 79,841). 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 dicyclohexyl-carbodiimide binding subunits of FOF1-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.
Tanaka
Y
Y
Chemical Tolerance, National Institute of Agrobiological Resources, Ibaraki, Japan.
Chiba
K
K
Maeda
M
M
Maeshima
M
M
D000595:Amino Acid Sequence; D001483:Base Sequence; D001693:Biological Transport, Active; D003001:Cloning, Molecular; D001467:Hordeum / Q000201:enzymology / Q000235:genetics*; D008565:Membrane Proteins / Q000737:chemistry / Q000235:genetics*; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000235:genetics*; D011755:Pyrophosphatases / Q000737:chemistry / Q000235:genetics*; D016415:Sequence Alignment; D012995:Solubility; D014617:Vacuoles
D008565:Membrane Proteins; D010940:Plant Proteins; D011755:Pyrophosphatases