Folding, assembly, and stability of the major light-harvesting complex of higher plants, LHCII, in the presence of native lipids.

The influence of thylakoid lipids on the association kinetics and thermal stability of the major light-harvesting complex of photosytem II (LHCII) has been studied in vitro. The apoprotein, light-harvesting chlorophyll a/b-binding protein (Lhcb1), can be refolded and complexed with pigments in detergent solution even in the absence of lipids. Two thylakoid lipids, phosphatidyl glycerol and digalactosyl diacylglycerol, are known to interact specifically with LHCII in vivo. Here we show that both of these lipids, as well as monogalactosyl diacylglycerol, stabilize reconstituted LHCII toward thermal denaturation. Two slow kinetic phases are connected with the establishment of energy transfer between chlorophyll b and chlorophyll a and, thus, are thought to reflect the formation of the pigment-protein complex with tightly coupled chlorophylls. The lipids studied here all have the same effect on the rate of complex assembly in vitro and slow these two kinetic phases by the same degree. Both kinetic phases also slow when reactant concentrations are decreased, suggesting that the corresponding reaction step(s) involve(s) pigment binding.