Abstract
Blue-native (BN) PAGE is a powerful tool for size separation of membrane protein complexes, since it is sensitive and mild method, which does not require additional detergents in the analytical system after solubilization. We demonstrated by BN-PAGE that n-dodecyl-β-D-maltoside (DM) stabilizes dimerization of photosystem II of Thermosynechococcus elongatus. In this study, we investigated a supramolecular organization of photosystems I and II (PSI and PSII) in mesophilic cyanobacteria and some eukaryotic algae. Thylakoid membranes were solubilized with DM and subjected to BN-PAGE. The PSII complexes were separated into the monomer and the dimer like in T. elongatus. On the other hand, there were unexpected variations in the organization of the PSI supercomplexes depending on the species. We discuss a variety of the PSI supramolecular organization.
