Arabidopsis ACBP6 is an acyl-CoA-binding protein associated with phospholipid metabolism.

In our recent paper in Plant Physiology, we showed that the Arabidopsis thaliana 10-kD acyl-CoA-binding protein, ACBP6, is subcellularly localized to the cytosol and that the overexpression of ACBP6 in transgenic Arabidopsis enhanced freezing tolerance. ACBP6-conferred freezing tolerance was independent of induced cold-regulated (COLD-RESPONSIVE) gene expression, but was correlated to an enhanced expression of phospholipase Ddelta (PLDdelta). Lipid analyses on cold-acclimated freezing-treated ACBP6-overexpressors revealed a decline in phosphatidylcholine (PC) and an elevation of phosphatidic acid (PA) in comparison to wild type. Furthermore, the His-tagged ACBP6 recombinant protein was observed using in vitro filter-binding assays to bind PC, but not PA or lysophosphatidylcholine. Taken together, our results implicate roles for ACBP6 in phospholipid metabolism that is related to gene regulation and PC-binding/transfer. This represents the first report demonstrating the in vitro binding of an ACBP to a phospholipid. The effect of ACBP6 on PLDdelta expression is reminiscent of yeast 10-kD ACBP function in the regulation of genes associated with stress responses, fatty acid synthesis and phospholipid synthesis. However, the yeast ACBP regulates the expression of genes involved in phospholipid synthesis by donation of acyl-CoA esters and its binding to phospholipids remains to be demonstrated.