Plant Physiol. Journal of Pharmacology and Experimental Therapeutics
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Published on August 20, 2008; 10.1104/pp.108.120436

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Received April 3, 2008
Accepted August 15, 2008

Discrete and Essential Roles of the Multiple Domains of Arabidopsis FHY3 in Mediating Phytochrome A Signal Transduction

Rongcheng Lin , Yibo Teng , Hee-Jin Park , Lei Ding , Christopher Black , Ping Fang , and Haiyang Wang *

Boyce Thompson Institute for Plant Research, Cornell University, Ithaca, NY 14853, USA; College of Environmental and Resources Sciences, Zhejiang University, Hangzhou, P.R. China

* Corresponding author; email: hw75{at}cornell.edu.

Phytochrome A (phyA) is the primary photoreceptor for mediating various far-red light induced responses in higher plants. We recently showed that Arabidopsis FHY3 and FAR1, a pair of homologous proteins sharing significant sequence homology to Mutator-like transposases, act as novel transcription factors essential for activating the expression of FHY1 and FHL, whose products are required for light-induced phyA nuclear accumulation and subsequent light responses. FHY3, FAR1 and Mutator-like transposases also share a similar domain structure, including an N-terminal C2H2 zinc-finger domain, a central putative core transposase domain, and a C-terminal SWIM motif. In this study, we performed a promoter-swapping analysis of FHY3 and FAR1. Our results suggest that the partially overlapping function of FHY3 and FAR1 entails divergence of their promoter activities and protein sub-functionalization. To gain a better understanding of the molecular mode of FHY3 function, we performed a structure-function analysis, using site-directed mutagenesis and transgenic approaches. We show that the conserved N-terminal C2H2 zinc-finger domain is essential for direct DNA binding and biological function of FHY3 in mediating light signaling, whereas the central core transposase domain and C-terminal SWIM domain are essential for the transcriptional regulatory activity of FHY3 and its homodimerization or hetero-dimerization with FAR1. Further, the ability to form homo- or hetero-dimers largely correlates with the transcriptional regulatory activity of FHY3 in plant cells. Together, our results reveal discrete roles of the multiple domains of FHY3 and provide functional support for the proposition that FHY3 and FAR1 represent transcription factors derived from a Mutator-like transposase(s).






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