The lipoproteins of cyanobacterial photosystem II

Photosystem II (PSII) complexes from cyanobacteria and plants perform water splitting and plastoquinone reduction and yet have a different complement of lumenal extrinsic proteins. Whereas PSII from all organisms has the PsbO extrinsic protein, crystal structures of PSII from cyanobacteria have PsbV and PsbU while green algae and higher plants instead contain the extrinsic PsbP and PsbQ subunits. Proteomic studies in Synechocystis sp. PCC 6803 identified three further extrinsic proteins in the thylakoid lumen that are associated with cyanobacterial PSII and these are predicted to attach to the thylakoid membrane via a lipidated N-terminus. These proteins are cyanobacterial homologues to the PsbP and PsbQ subunits as well as to Psb27, an additional extrinsic protein associated with “inactive” photosystems that lack the other extrinsic polypeptides. The PsbQ homologue is not present in Prochlorococcus species but otherwise these proteins have been identified in most cyanobacteria although our phylogenetic analyses identified some strains that lack an apparent motif for lipidation in one or other of these subunits. Over the past decade the physiological function of these additional lipoproteins has been investigated in several cyanobacterial strains and recently the structures for each have been solved. This review will evaluate the physiological and structural results obtained for these lipid-attached extrinsic proteins and in silico protein docking of these proteins to PSII centers will be presented.