Plant Physiology Preview
Published on September 7, 2007; 10.1104/pp.107.105601
OPEN ACCESS ARTICLE
Received July 17, 2007
Accepted August 29, 2007
Phytochrome Induces Rapid PIF5 Phosphorylation and Degradation in Response to Red-light Activation
Yu Shen , Rajnish Khanna , Christine M. Carle , and Peter H. Quail *
Department of Plant and Microbial Biology, University of California, Berkeley, CA 94720; and USDA/ARS-Plant Gene Expression Center, 800 Buchanan Street, Albany, CA 94710
* Corresponding author; email: quail{at}nature.berkeley.edu.
The phytochrome (phy) family of sensory photoreceptors (phyA to phyE in Arabidopsis) induce changes in target-gene expression upon light-induced translocation to the nucleus, where certain members interact with selected members of the constitutively-nuclear basic helix-loop-helix (bHLH) transcription factor family, such as PHYTOCHROME-INTERACTING FACTOR 3 (PIF3). Previous evidence indicates that the binding of the photoactivated photoreceptor molecule to PIF3 induces rapid phosphorylation of the transcription factor in the cell prior to its degradation via the ubiqitin-proteosome system. To investigate whether this apparent primary signaling mechanism can be generalized to other phy-interacting partners, we have examined the molecular behavior of a second related phy-interacting member of the bHLH family, PIF5, during early deetiolation, immediately following initial exposure of dark-grown seedlings to light. The data show that red light induces very rapid phosphorylation and subsequent degradation (t1/2 <5 min) of PIF5 via the proteosome system upon irradiation. Photobiological and genetic evidence indicates that the photoactivated phy molecule acts within 60 s to induce this phosphorylation of PIF5, and that phyA and phyB redundantly dominate this process, with phyD playing an apparently minor role. Collectively, the data support the proposal that the rapid phy-induced phosphorylation of PIF3 and PIF5 may represent the biochemical mechanism of primary signal transfer from photoactivated photoreceptor to binding partner, and that phyA and phyB (and possibly phyD) may signal to multiple, shared partners utilizing this common mechanism.
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