cDNA Cloning of a Vacuolar H^+-Pyrophosphatase and Its Expression in Hordeum brevisubulatum (Trin.) Link in Response to Salt Stress  

作　　者：LUEShi-you JINGYu-xiang PANGXiao-bin ZHAOHua-yan MALan-qing LIYan-fang 

机构地区：[1]CollegeofPlantScience,JilinUniversity,Changchun130062,P.R.China [2]KeyLaboratoryofPlantPhotosynthesisandEnvironmentalMolecularPhysiology,InstituteofBotany,ChineseAcademyofSciences,Beijing100093,P.R.China

出　　处：《Agricultural Sciences in China》2005年第4期247-251,共5页中国农业科学（英文版）

基　　金：This work was supported by the National Natural Science Foundation of China(30471229)

摘　　要：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.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.

关 键 词：Hordeum brevisubulatum HbVP1 Salt tolerance 

分 类 号：S512.3[农业科学—作物学]