Light-induced phosphorylation and degradation of the negative regulator PIF1 depends upon its direct physical interactions with photoactivated phytochromes
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Title |
Light-induced phosphorylation and degradation of the negative regulator PIF1 depends upon its direct physical interactions with photoactivated phytochromes
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Creator |
Shen, Hui
Zhu, Ling Castillon, Alicia Majee, Manoj Downie, Bruce Huq, Enamul |
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Subject |
phytochrome
photoreceptors Arabidopsis Photoactivated Phosphorylation Light-Induced |
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Description |
The phytochrome (phy) family of photoreceptors regulates changes in gene expression in response to red/far-red light signals in part by physically interacting with constitutively nucleus-localized phy-interacting basic helix-loop-helix transcription factors (PIFs). Here, we show that PIF1, the member with the highest affinity for phys, is strongly sensitive to the quality and quantity of light. phyA plays a dominant role in regulating the degradation of PIF1 following initial light exposure, while phyB and phyD and possibly other phys also influence PIF1 degradation after prolonged illumination. PIF1 is rapidly phosphorylated and ubiquitinated under red and far-red light before being degraded with a half-life of ~1 to 2 min under red light. Although PIF1 interacts with phyB through a conserved active phyB binding motif, it interacts with phyA through a novel active phyA binding motif. phy interaction is necessary but not sufficient for the light-induced phosphorylation and degradation of PIF1. Domain-mapping studies reveal that the phy interaction, light-induced degradation, and transcriptional activation domains are located at the N-terminal 150–amino acid region of PIF1. Unlike PIF3, PIF1 does not interact with the two halves of either phyA or phyB separately. Moreover, overexpression of a light-stable truncated form of PIF1 causes constitutively photomorphogenic phenotypes in the dark. Taken together, these data suggest that removal of the negative regulators (e.g., PIFs) by light-induced proteolytic degradation might be sufficient to promote photomorphogenesis. This work was supported by National Science Foundation Grant MCB-0449646 to B.D. and by National Science Foundation Grant IBN-0418653 and a set-up fund from the University of Texas at Austin to E.H. |
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Date |
2013-11-12T06:22:07Z
2013-11-12T06:22:07Z 2008 21 May 2008 |
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Type |
Article
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Identifier |
Plant Cell, 20(6): 1586-1602
http://hdl.handle.net/123456789/101 |
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Language |
en
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Publisher |
American Society of Plant Biologists
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