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http://purl.uniprot.org/citations/15805487http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15805487http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15805487http://www.w3.org/2000/01/rdf-schema#comment"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 beta-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."xsd:string
http://purl.uniprot.org/citations/15805487http://purl.org/dc/terms/identifier"doi:10.1105/tpc.104.029645"xsd:string
http://purl.uniprot.org/citations/15805487http://purl.org/dc/terms/identifier"doi:10.1105/tpc.104.029645"xsd:string
http://purl.uniprot.org/citations/15805487http://purl.uniprot.org/core/author"Rubio V."xsd:string
http://purl.uniprot.org/citations/15805487http://purl.uniprot.org/core/author"Rubio V."xsd:string
http://purl.uniprot.org/citations/15805487http://purl.uniprot.org/core/author"Sang Y."xsd:string
http://purl.uniprot.org/citations/15805487http://purl.uniprot.org/core/author"Sang Y."xsd:string
http://purl.uniprot.org/citations/15805487http://purl.uniprot.org/core/author"Deng X.-W."xsd:string
http://purl.uniprot.org/citations/15805487http://purl.uniprot.org/core/author"Deng X.-W."xsd:string
http://purl.uniprot.org/citations/15805487http://purl.uniprot.org/core/author"Yang H.-Q."xsd:string
http://purl.uniprot.org/citations/15805487http://purl.uniprot.org/core/author"Yang H.-Q."xsd:string
http://purl.uniprot.org/citations/15805487http://purl.uniprot.org/core/author"Mao J."xsd:string
http://purl.uniprot.org/citations/15805487http://purl.uniprot.org/core/author"Mao J."xsd:string
http://purl.uniprot.org/citations/15805487http://purl.uniprot.org/core/author"Zhang Y.-C."xsd:string
http://purl.uniprot.org/citations/15805487http://purl.uniprot.org/core/author"Zhang Y.-C."xsd:string
http://purl.uniprot.org/citations/15805487http://purl.uniprot.org/core/author"Li Q.-H."xsd:string
http://purl.uniprot.org/citations/15805487http://purl.uniprot.org/core/author"Li Q.-H."xsd:string
http://purl.uniprot.org/citations/15805487http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15805487http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15805487http://purl.uniprot.org/core/name"Plant Cell"xsd:string
http://purl.uniprot.org/citations/15805487http://purl.uniprot.org/core/name"Plant Cell"xsd:string
http://purl.uniprot.org/citations/15805487http://purl.uniprot.org/core/pages"1569-1584"xsd:string
http://purl.uniprot.org/citations/15805487http://purl.uniprot.org/core/pages"1569-1584"xsd:string