Molecular cloning and partial characterization of a novel phospholipase D gene from Chorispora bungeana
Molecular cloning and partial characterization of a novel phospholipase D gene from Chorispora bungeana
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DOI：
10.1007/s11240-011-0029-1
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发表时间：
2011-09
期刊：
影响因子：
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通讯作者：
N. Yang;bullet X L Yue;bullet X L Chen;G. F. Wu;bullet T G Zhang;bullet L Z An
中科院分区：
文献类型：
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作者：
N. Yang;bullet X L Yue;bullet X L Chen;G. F. Wu;bullet T G Zhang;bullet L Z An
Chorispora bungeanaFisch。而chispora bungeana是一种罕见的高寒亚寒植物，对环境胁迫具有高度的耐受性。磷脂酶D （Phospholipase D， PLD）是植物生长发育和逆境响应过程中参与膜磷脂分解代谢的关键酶。我们从白毛菜（chorispora bungeana， C.）的愈伤组织中分离并部分鉴定了编码PLD的全长cDNA。bungeana)，目的是进一步了解PLD在分子水平上的作用。TheC。发现bungeanaPLD编码一个903个氨基酸的蛋白，其核苷酸序列与先前报道的植物PLD β基因相似。预测的CbPLD序列分别显示具有钙敏感性的C2结构域和具有酶活性的磷脂酶结构域。CbPLD转录本在低温（4℃和- 4℃）、ABA、盐度、过氧化氢（H2O2）和高温处理下均有较高的积累。这些结果表明，CbPLD可能在白豆对胁迫的响应中起重要作用。
Chorispora bungeanaFisch. and C.A. Mey (Chorispora bungeana) is a rare alpine subnival plant species that is highly tolerant to environmental stress. Phospholipase D (PLD) is a key enzyme involved in membrane phospholipid catabolism during plant growth, development and stress responses. We have isolated and partially characterized a full-length cDNA encoding PLD from the calluses ofChorispora bungeana(C. bungeana), with the aim of furthering our understanding of the role of PLD at the molecular level. TheC. bungeanaPLD was found to encode a 903-amino acid protein with moderate to high nucleotide sequence similarity to previously reported plant PLD beta genes. The predicted CbPLD sequence showed the characteristic C2 domain and the phospholipase domains conferring calcium sensitivity and the enzyme activity, respectively. The transcripts of CbPLD accumulated highly whenChorispora bungeanawas treated with cold (4 and −4°C), abscisic acid (ABA), salinity, hydrogen peroxide (H2O2) and heat. These results indicate that the CbPLD may play an important role in response to stresses inChorispora bungeana.