Efficiency of phospholipid remodeling via acyl-CoA:lysophospholipid acyltransferases action is modified by acyl-CoAs

This study investigated the impact of different acyl-CoAs on remodeling efficiency of PC and PE via the action of acyl-CoA:lysophospholipid acyltransferases (LPLAT). Microsomal fractions from yeast & UDelta;ALE1 mutant transformed with an empty plasmid pYES2 or plasmid carrying AtLPCAT or ALE1 encoding genes were used in the experiments. In the preliminary assays, presence of 18:1-CoA in the reaction mixture increased remodeling efficiency of [C-14]PC integrated with microsomal fraction of yeast overexpressing AtLPCAT compared to assays without exogenous acyl-CoA. In further experiments, the effect of five different acyl-CoAs (16:0-CoA, 18:0-CoA, 18:1-CoA, 18:2-CoA, and 18:3-CoA) on remodeling efficiency of yeast microsomal PC and PE via the action of three LPLATs (yeast SLC1 and ALE1 and Arabidopsis LPCAT2) were tested. It has been shown that acyl-CoAs used in the experiments had different effect on the remodeling intensity of PC and PE via action of the tested acyltransferases. Moreover, each acyl-CoA used had a different effect on the tested acyltransferases. Additionally, the assays with DTNB (inhibitor of the LPLAT backward reaction) showed that remodeling of PC and PE by LPLATs can also occur through reactions other than the backward reaction carried out by these enzymes, and that acyl-CoA present in the reaction mixture affected these processes.