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《农业科学学报：英文版》
>cDNA Cloning of a Vacuolar H^+-Pyrophosphatase and Its Expression in Hordeum brevisubulatum (Trin.) Link in Response to Salt Stress
cDNA Cloning of a Vacuolar H^+-Pyrophosphatase and Its Expression in Hordeum brevisubulatum (Trin.) Link in Response to Salt Stress
A cDNA clone encoding a vacuolar H+-pyrophosphatase (V-H+-PPase) was isolated from Hordeum brevisubulatum (Trin.) Link by using RACE method. Sequence analysis revealed that HbVP1 contained 2 319 nucleotides of open reading frame (ORF) and 420 nucleotides of 3′-untranslated region. Its encoding protein consisted of 773 amino acid residues, which includes 14 transmembrane helices. The predicated molecular mass is 80.4 kDa with pI of 4.90. The V-H+-PPases in higher plants shared low identity (40-55%) with those of protozoa, marine alga and archaebacteria. HbVP1 transcripts accumulated abundantly in roots, shoots and seeds, and it was also strongly induced by salt treatment.
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