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Plant Cell Advance Online Publication
Published on February 10, 2009; 10.1105/tpc.108.061259

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Received June 5, 2008
Returned for revision January 8, 2009
Accepted January 20, 2009

Phytochrome A Mediates Rapid Red Light–Induced Phosphorylation of Arabidopsis FAR-RED ELONGATED HYPOCOTYL1 in a Low Fluence Response

Yunping Shen 1, Zhenzhen Zhou 2, Suhua Feng 3, Jigang Li 3, Anna Tan-Wilson 4, Li-Jia Qu 5, Haiyang Wang 6, and Xing Wang Deng 1*

1 Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, Connecticut, 06520-8104; Peking-Yale Joint Center of Plant Molecular Genetics and Agrobiotechnology, College of Life Sciences, Peking University, Beijing 100871, China
2 Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, Connecticut, 06520-8104; Department of Biological Sciences, State University of New York, Binghamton, New York, 13902-6000
3 Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, Connecticut, 06520-8104
4 Department of Biological Sciences, State University of New York, Binghamton, New York, 13902-6000
5 Peking-Yale Joint Center of Plant Molecular Genetics and Agrobiotechnology, College of Life Sciences, Peking University, Beijing 100871, China
6 Boyce Thompson Institute for Plant Research, Cornell University, Ithaca, New York 14853

* To whom correspondence should be addressed. E-mail: xingwang.deng{at}yale.edu.

Phytochrome A (phyA) is the primary photoreceptor for mediating the far-red high irradiance response in Arabidopsis thaliana. FAR-RED ELONGATED HYPOCOTYL1 (FHY1) and its homolog FHY1-LIKE (FHL) define two positive regulators in the phyA signaling pathway. These two proteins have been reported to be essential for light-regulated phyA nuclear accumulation through direct physical interaction with phyA. Here, we report that FHY1 protein is phosphorylated rapidly after exposure to red light. Subsequent exposure to far-red light after the red light pulse reverses FHY1 phosphorylation. Such a phenomenon represents a classical red/far-red reversible low fluence response. The phosphorylation of FHY1 depends on functioning phyA but not on other phytochromes and cryptochromes. Furthermore, we demonstrate that FHY1 and FHL directly interact with phyA by bimolecular fluorescence complementation and that both FHY1 and FHL interact more stably with the Pr form of phyA in Arabidopsis seedlings by coimmunoprecipitation. Finally, in vitro kinase assays confirmed that a recombinant phyA is able to robustly phosphorylate FHY1. Together, our results suggest that phyA may differentially regulate FHY1 and FHL activity through direct physical interaction and red/far-red light reversible phosphorylation to fine-tune their degradation rates and resulting light responses.




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S. W. Yang, I.-C. Jang, R. Henriques, and N.-H. Chua
FAR-RED ELONGATED HYPOCOTYL1 and FHY1-LIKE Associate with the Arabidopsis Transcription Factors LAF1 and HFR1 to Transmit Phytochrome A Signals for Inhibition of Hypocotyl Elongation
PLANT CELL, May 1, 2009; 21(5): 1341 - 1359.
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