Cryo-EM structure of photosystem II supercomplex from Chlorella ohadii, a green microalga with extreme phototolerance

Photosystem II (PSII) is essential for energy conversion during oxygenic photosynthesis in plants and algae. Chlorella ohadii, one of the fastest multiplying green alga, thrives under the harsh desert sun but lacks the standard PSII photoprotective mechanisms involving LhcSR/PsbS proteins or protein phosphorylation. Here, we present analysis of cryo-EM structure of the PSII supercomplex from C. ohadii at 2.9Å resolution to determine whether the exceptional resistance to desert conditions has a structural basis in PSII. The structure reveals a novel PsbO isoform and additional subunits, PsbR and PsbY, which enhance core complex stability through extensive interactions. Furthermore, the trimeric light-harvesting complexes (LHCII) are bound to the PSII core by specific light-harvesting proteins whose down-regulation in response to high light conditions implies a reduction in the number of bound LHCII trimers. These modifications play a crucial role in maintaining PSII stability and photoprotection, allowing C. ohadii to survive in extreme conditions.