The CRY1 Blue Light Photoreceptor of Arabidopsis Interacts with Phytochrome A In Vitro
| Autor: | Jose A. Jarillo, Margaret Ahmad, Olga Smirnova, Anthony R. Cashmore |
|---|---|
| Rok vydání: | 1998 |
| Předmět: |
animal structures
Recombinant Fusion Proteins Mutant Arabidopsis Saccharomyces cerevisiae Phosphates Receptors G-Protein-Coupled Phytochrome A Cryptochrome Drosophila Proteins Photoreceptor Cells Kinase activity Phosphorylation Receptor Eye Proteins Molecular Biology Alleles Plant Proteins Genetics Phytochrome biology Flavoproteins Arabidopsis Proteins fungi Phosphotransferases Cell Biology biology.organism_classification Plants Genetically Modified Cell biology Cryptochromes Mutation Photoreceptor Cells Invertebrate sense organs Protein Binding |
| Zdroj: | Molecular Cell. 1(7):939-948 |
| ISSN: | 1097-2765 |
| DOI: | 10.1016/s1097-2765(00)80094-5 |
| Popis: | Plants have at least two major photosensory receptors: phytochrome (absorbing primarily red/far-red light) and cryptochrome (absorbing blue/UV-A light); considerable physiological and genetic evidence suggests some form of communication or functional dependence between the receptors. Here, we demonstrate in vitro, using purified recombinant photoreceptors, that Arabidopsis CRY1 and CRY2 (cryptochrome) are substrates for phosphorylation by a phytochrome A–associated kinase activity. Several mutations within the CRY1 C terminus lead to reduced phosphorylation by phytochrome preparations in vitro. Yeast two-hybrid interaction studies using expressed C-terminal fragments of CRY1 and phytochrome A from Arabidopsis confirm a direct physical interaction between both photoreceptors. In vivo labeling studies and specific mutant alleles of CRY1, which interfere with the function of phytochrome, suggest the possible relevance of these findings in vivo. |
| Databáze: | OpenAIRE |
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