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N-Terminal Domain–Mediated Homodimerization Is Required for Photoreceptor Activity of Arabidopsis CRYPTOCHROME 1

^a National Key Laboratory of Plant Molecular Genetics, Institute of Plant Physiology and Ecology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200032, China
^b Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, Connecticut 06520-8104

² To whom correspondence should be addressed. E-mail hqyang{at}sibs.ac.cn; fax 86-21-54924015.

Cryptochromes (CRY) are blue light receptors that share sequence similarity with photolyases, flavoproteins that catalyze the repair of UV light–damaged DNA. Transgenic Arabidopsis thaliana seedlings expressing the C-terminal domains of the Arabidopsis CRY fused to ß-glucuronidase (GUS) display a constitutive photomorphogenic (COP) phenotype, indicating that the signaling mechanism of Arabidopsis CRY is mediated through the C-terminal domain. The role of the Arabidopsis CRY N-terminal photolyase-like domain in CRY action remains poorly understood. Here, we report the essential role of the Arabidopsis CRY1 N-terminal domain (CNT1) in the light activation of CRY1 photoreceptor activity. Yeast two-hybrid assay, in vitro binding, in vivo chemical cross-linking, gel filtration, and coimmunoprecipitation studies indicate that CRY1 homodimerizes in a light-independent manner. Mutagenesis and transgenic studies demonstrate that CNT1-mediated dimerization is required for light activation of the C-terminal domain of CRY1 (CCT1). Transgenic data and native gel electrophoresis studies suggest that multimerization of GUS is both responsible and required for mediating a COP phenotype on fusion to CCT1. These results indicate that the properties of the GUS multimer are analogous to those of the light-modified CNT1 dimer. Irradiation with blue light modifies the properties of the CNT1 dimer, resulting in a change in CCT1, activating CCT1, and eventually triggering the CRY1 signaling pathway.

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