Location: Plant Physiology and Genetics ResearchTitle: Cloning of Phospholipase A2s from Lesquerella Fendleri) Author
Submitted to: Meeting Abstract
Publication Type: Abstract only
Publication Acceptance Date: 5/15/2010
Publication Date: 7/11/2010
Citation: Chen, G., Krishnamurthy, R., Mietkiewska, E., Snyder, C., Dyer, J.M., and Weselake, R. (2010). Cloning of Phospholipase A2s from Lesquerella Fendleri. International Symposium on Plant Lipids, July 11 - 16, 2010, Cairns, Australia. Interpretive Summary:
Technical Abstract: Wax esters containing hydroxy fatty acids would possess stellar lubricative properties, superior resistance to hydrolysis, high oxidative stability, and low-melting temperature. One of the obstacles, however, to attaining high levels of such wax esters in plants is the inefficient release of newly hydroxylated acyl moieties from phospholipids into the acyl-CoA pool. Phospholipase A2 (PLA2), which specifically cleaves the acyl group from the sn-2 position of phospholipids and releases a free fatty acid and a lysophospholipid may play a key role in this process. We are attempting to identify ricinoleoyl-specific PLA2s from developing seeds of Lesquerella fendleri, a crop which accumulates up to 60% hydroxy-fatty acids in its seed oil. Recently two LfPLA2 cDNA clones and their corresponding genes were isolated. To confirm the function of the proteins encoded by LfPLA2s, the coding regions were linked to the GAL1-inducible promoter in the yeast expression vector pYES2/NT and transformed into S. cerevisiae phospholipase B mutant strain. Currently, we are determining the substrate specificity properties of the PLA2s produced using the encoding cDNAs.