Abstract
Phosholipase A2(PLA2) hydrolyzes glycerophospholipids to produce free fatty acids and lysophospholipids. In animals, secreted PLA2s(sPLA2) have been recognized as a large super family of distinct enzymes that play a central role in diverse cellular processes. In plants, little is known about the biological functions of sPLA2, although there are some reports of purification and cDNA cloning of sPLA2. To investigate biological function of sPLA2 in tobacco, Nicotiana tabacum, we attempted to isolate cDNAs for sPLA2 from tobacco. Initially, we performed RT-PCR with primes selected on highly conserved regions of sPLA cDNAs using total RNA extracted from tobacco flower. Next, we performed 5'- and 3'-RACE using gene-specific primers derived from the respective partial sequences. The cDNAs of sPLA2 from tobacco encoded 145 and 159 amino acids, respectively. The deduced amino acid sequences were shown to have a putative signal peptide. At present, we have studied gene expression of sPLA2 in tobacco.
