Abstract
The phytochrome photoreceptor family directs plant gene expression by switching between biologically inactive and active conformers in response to the sequential absorption of red and far-red photons1,2. Several intermediates that act late in the phytochrome signalling pathway have been identified, but fewer have been identified that act early in the pathway3,4. We have cloned a nuclear basic helix–loop–helix protein, PIF3, which can bind to non-photoactive carboxy-terminal fragments of phytochromes A and B and functions in phytochrome signalling in vivo5. Here we show that full-length photoactive phytochrome B binds PIF3 in vitro only upon light-induced conversion to its active form, and that photoconversion back to its inactive form causes dissociation from PIF3. We conclude that photosensory signalling by phytochrome B involves light-induced, conformer-specific recognition of the putative transcriptional regulator PIF3, providing a potential mechanism for direct photoregulation of gene expression.
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Acknowledgements
We thank C. Fairchild for the gift of phycocyanobilin; C. Fairchild, M. Hudson, E.Huq, J. Martinez and E. Monte for critical reading of the manuscript; lab members for discussion and support; and R. Wells for help with the manuscript. This work was supported by grants from the DOG and USDA.
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Ni, M., Tepperman, J. & Quail, P. Binding of phytochrome B to its nuclear signalling partner PIF3 is reversibly induced by light. Nature 400, 781–784 (1999). https://doi.org/10.1038/23500
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DOI: https://doi.org/10.1038/23500
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