Fig. 3

Commonly used photoactivatable systems. Brief scheme of properties and conformational changes of several photoactivatable systems. Here we use POI (protein of interest) to represent the effectors fused to the photoactivatable protein. a Phy-PIF system: Exposure to FR (640–680 nm) light induces association of PIF and Phy, while exposure to NIR (740–780 nm) light induces dissociation of PIF from Phy. b DrBphP system: Under NIR (740–780 nm) light, DrBphP can form homodimers. After Absorption of FR (640–680 nm) light, DrBphP dimers come apart. c BLUF system: Blue light (~ 450 nm) can trigger conformational change of BLUF and expose/activate POI. d LOV2/Jα system: Interaction between Light-sensitive LOV2 domain of and Jα helix can be reversibly disrupted by blue light (~ 450 nm). e LOV2TRAP system: Zdk binds selectively to the dark state of LOV2, which can be separated apart by blue light (~ 450 nm). f LOV2-LOV2 system: LOV2 form homo-dimerization upon blue light stimulation (~ 450 nm). g CRY2-CIB1 system: Exposure to blue (~ 450 nm) light induces association of CRY2 and CIB1. h CRY2 oligomerization: In the presence of blue light (~ 450 nm), photoexcited CRY2 undergoes photoreduction to adopt an open conformation, leading to the formation of CRY2 homodimers and homo-oligomers. i LOV2 form homo-dimerization at dark state, which come apart upon UV light (~ 300 nm)