Studies of phospholipid binding to N-terminal domain of membrane protein light-harvesting complex II

The peptide fragment of the light harvesting complex II comprising the trim erisation site binds strongly and selectively to phosphatidylglycerol while the affinity to the other LHCII-bound lipid digalactosyldiacylglycerol is negligible. Upon its binding, large aggregates of the lipid are formed whic h do not occur in the presence of other peptides, in particular the peptide comprising the phosphorylation site. Our observation supports a hypothesis that the trimerisation site of LHCII is also the specific binding site for phosphatidylglycerol and favors another hypothesis that the phosphorylatio n site is directly involved in the control of trimerisation. (C) 2000 Elsev ier Science B.V. All rights reserved.