The key cyclic electron flow protein PGR5 associates with cytochrome b(6)f, and its function is partially influenced by the LHCII state transition

In plants and algae, PGR5-dependent cyclic electron flow (CEF) is an important regulator of acclimation to fluctuating environments, but how PGR5 participates in CEF is unclear. In this work, we analyzed two PGR5s in cucumber (Cucumis sativus L.) under different conditions and found that CsPGR5a played the dominant role in PGR5-dependent CEF. The results of yeast two-hybrid, biomolecular fluorescence complementation (BiFC), blue native PAGE, and coimmunoprecipitation (CoIP) assays showed that PGR5a interacted with PetC, Lhcb3, and PsaH. Furthermore, the intensity of the interactions was dynamic during state transitions, and the abundance of PGR5 attached to cyt b(6)f decreased during the transition from state 1 to state 2, which revealed that the function of PGR5a is related to the state transition. We proposed that PGR5 is a small mobile protein that functions when attached to protein complexes. Two PGR5s are present in some species of algae and higher plants, and CsPGR5a plays the dominant role in PGR5-dependent cyclic electron flow in cucumber. PGR5 is a small and mobile protein that functions when attached to protein complexes. In this study, the function of PGR5 was found to be partially related to the state transition.