Binding of phytochrome B to its nuclear signalling partner PIF3 is reversibly induced by light

Min Ni, James M. Tepperman and Peter H. Quail ()
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Min Ni: University of California
James M. Tepperman: University of California
Peter H. Quail: University of California

Nature, 1999, vol. 400, issue 6746, 781-784

Abstract: 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.

Date: 1999
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DOI: 10.1038/23500

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