Molecular cloning and partial characterization of a novel phospholipase D gene from Chorispora bungeana

Chorispora bungeana Fisch. 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 of Chorispora bungeana (C. bungeana), with the aim of furthering our understanding of the role of PLD at the molecular level. The C. bungeana PLD 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 when Chorispora bungeana was treated with cold (4 and -4A degrees C), abscisic acid (ABA), salinity, hydrogen peroxide (H(2)O(2)) and heat. These results indicate that the CbPLD may play an important role in response to stresses in Chorispora bungeana.