Conformational change induced by ATP binding correlates with enhanced biological function of Arabidopsis cryptochrome.

Cryptochromes are widely distributed blue light photoreceptors involved in numerous signaling functions in plants and animals. Both plant and animal-type cryptochromes are found to bind ATP and display intrinsic autokinase activity; however the functional significance of this activity remains a matter of speculation. Here we show in purified preparations of Arabidopsis cry1 that ATP binding induces conformational change independently of light and increases the amount and stability of light-induced flavin radical formation. Nucleotide binding may thereby provide a mechanism whereby light responsivity in organisms can be regulated through modulation of cryptochrome photoreceptor conformation.

Multiple interactions between cryptochrome and phototropin blue-light signalling pathways in Arabidopsis thaliana.

Higher plants contain two structurally unrelated flavoprotein blue-light photoreceptors, the cryptochromes and the phototropins, which mediate largely distinct response pathways. Cryptochromes regulate plant development and photomorphogenesis whereas phototropins are primarily implicated in photomovement responses such as phototropism and chloroplast relocation. In the present study we identify interactions between cryptochromes and phototropins in several photoresponses of Arabidopsis thaliana. Cryptochromes are shown to exert a positive effect on phototropic curvature under long-term irradiation conditions. Specifically, in a phot1-deficient genetic background (phot1 mutant), curvature is reduced in the absence of cryptochromes, particularly at wavelengths where cryptochromes show preferential absorption. Phototropins in turn exert a small promotive effect on such cryptochrome-mediated responses as hypocotyl elongation and anthocyanin accumulation. These effects are apparent in a cryptochrome-deficient (cry1cry2 mutant) genetic background. In addition to positive interactions between signalling pathways, we demonstrate that the cryptochromes also exert a negative regulatory effect. Levels of phot1 protein decrease in blue light as a function of cryptochrome photoreceptor activation. This negative regulation occurs in part at the level of phot1 transcription but may also involve post-transcriptional mechanisms. These two classes of photoreceptor thereby reciprocally modulate their overall responsivity to blue light through multiple forms of interaction.