Architecture and functional regulation of a plant PSII-LHCII megacomplex.

Abstract

Photosystem II (PSII) splits water in oxygenic photosynthesis on Earth. The structure and function of the C₄S₄M₂-type PSII-LHCII (light-harvesting complex II) megacomplexes from the wild-type and PsbR-deletion mutant plants are studied through electron microscopy (EM), structural mass spectrometry, and ultrafast fluorescence spectroscopy [time-resolved fluorescence (TRF)]. The cryo-EM structure of a type I C₄S₄M₂ megacomplex demonstrates that the three domains of PsbR bind to the stromal side of D1, D2, and CP43; associate with the single transmembrane helix of the redox active Cyt <i>b</i>₅₅₉; and stabilize the luminal extrinsic PsbP, respectively. This megacomplex, with PsbR and PsbY centered around the narrow interface between two dimeric PSII cores, provides the supramolecular structural basis that regulates the plastoquinone occupancy in Q_B site, excitation energy transfer, and oxygen evolution. PSII-LHCII megacomplexes (types I and II) and LHC aggregation levels in <i>Arabidopsis psbR</i> mutant were also interrogated and compared to wild-type plants through EM and picosecond TRF.