Nearest-neighbor analysis of a photosystem II complex from Marchantia polymorpha L. (liverwort), which contains reaction center and antenna proteins.

A new photosystem II preparation was isolated from Marchantia polymorpha thylakoids upon solubilization with dodecyl beta-D-maltoside and glycerol gradient ultracentrifugation. Its protein composition was analyzed, and all tested polypeptides from the core complex, the oxygen-evolving enhancer and the light-harvesting complex (LHC) could be detected. The only component severely depleted compared with the grana membrane preparation was the psbS gene product. This complex was subjected to chemical cross-linking using the cleavable homobifunctional cross-linker dithiobis(sulfosuccinimidylpropionate). The overall pattern of cross-linking-products was analyzed by diagonal electrophoresis, where the cross-linking agent was cleaved by reduction of the disulfide bond between the first and second dimensions of the gel, followed by immunoblotting. Many cross-linking products were characterized and these data used in order to identify protein masses revealed by electron microscopy [Boekema, E. J., Hankamer, B., Bald, D., Kruip, J., Nield, J., Boonstra, A. F., Barber, J. & Rögner, M. (1995) Proc. Natl Acad. Sci. USA 92, 175-179]. It is concluded that the core proteins CP43 and CP47 are located at opposite sides of the D1-D2-cytochrome b559 complex. Minor CAB proteins were found to interact with core complex subunits (CP29, CP26) and LHCII (CP26), supporting the view that these proteins could interface the major LHCII with the reaction center.