Effects of histone and diolein on the structure of phosphatidylcholine/phosphatidylserine or phosphatidylcholine/phosphatidylglycerol bilayers.

Abstract

The effects of the PKC substrate histone 1 and the PKC activator diolein (Ole2Gro) on the structure of phosphatidylcholine (PtdCho)/phosphatidylserine (PtdSer), or PtdCho/phosphatidylglycerol (PtdGro) bilayers were studied using 2H-NMR. The results showed that in PtdCho/PtdSer bilayers, histone preferentially increased order parameters of the acyl chains of the PtdSer, but not the PtdCho lipid component. This effect was additive with the effect of Ole2Gro, which equally increased the ordering of the acyl chains of both PtdCho and PtdSer. The histone-induced change in the conformation of the PtdCho headgroups in PtdCho/PtdSer bilayers indicated that positively charged residues of the bound histone are located above the lipid-water interface and their location was altered by the presence of Ole2Gro. A different picture was observed in the case of PtdCho/PtdGro bilayers; although the effect of Ole2Gro on both the PtdCho or the PtdGro components was similar to the case of the PtdCho/PtdSer bilayers, histone did not significantly affect the order parameters of PtdCho or PtdGro in either the absence or presence of Ole2Gro. The results indicate that histone 1 induces clustering of PtdSer in PtdCho bilayers which may contribute to PKC activation. Moreover, the observed differences in the interactions of histone with PtdCho/PtdSer compared with PtdCho/PtdGro bilayers may explain the higher efficiency of PtdSer in activating PKC.