THE PSII-S PROTEIN OF HIGHER-PLANTS - A NEW-TYPE OF PIGMENT-BINDING PROTEIN

An intrinsic 22 kDa protein of photosystem II has been shown to possess high sequence homology with the CAB gene products, but differs from these proteins by an additional putative fourth transmembrane helix. This protein, designated PSII-S in accordance with the assignment of the name psbS to its gene, has been isolated by nonionic detergents and preparative isoelectric focusing in this study. The isolated PSII-S protein was shown to bind 5 chlorophyll molecules (a and b) per protein unit and also several different kinds of carotenoids. The room temperature absorption spectrum of the Q(y) transition of the chlorophylls bound to the isolated protein is characterized by a broad band with a maximum at 671 nm. The 77 K fluorescence spectrum exhibits a peak at 672 nm. A single photon counting technique was applied to resolve the room temperature decay kinetics of the first excited singlet states in the chlorophyll ensemble of the PSII-S protein. The data can be satisfactorily described by triexponential kinetics with lifetimes of tau(1) = 1.8 ns, tau(2) = 4.4 ns, and tau(3) = 6.1 ns and normalized amplitudes of 0.09, 0.60, and 0.31, respectively. Circular dichroism spectra suggest that, in contrast to LHCII, virtually no pigment coupling exists in the PSII-S protein. Two copies of the PSII-S protein were found per PSII in spinach thylakoids. It displays an unusually extreme lateral heterogeneity, since the PSII beta centers located in the stroma exposed thylakoid regions contained only residual amounts of the PSII-S protein. Although the protein is unambiguously shown to bind pigments, it has several features distinct from previously described chlorophyll binding proteins. Therefore, it seems very likely that the PSII-S protein is involved in additional and/or alternative functions to normal light-harvesting.