Phospholipase Dα from Chorispora bungeana: cloning and partial functional characterization

Abstract

Chorispora bungeana Fisch. and C.A. Mey (C. 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 PLDα from the plantlets in vitro of C. bungeana, with the aim of furthering our understanding of the role of PLDα at the molecular level. The C. bungeana PLDα (CbPLDα) was found to encode a 810-amino acid protein with moderate to high nucleotide sequence similarity to previously reported plant PLDα genes. RT-PCR analyses suggested that CbPLDα gene expression is correlated with the CbPLDα activity when C. bungeana plantlets were treated with low temperature (4, 0 and −4 °C). Furthermore, the CbPLDα gene was found to be expressed at high levels in leaf and root tissues. These results indicate that the CbPLDα may play an important role in response to low temperature stresses in C. bungeana.