Phytochrome Phosphorylation Modulates Light Signaling by Influencing the Protein–Protein Interaction<sup><a href="#fn2" rid="fn2" class=" fn">W⃞</a></sup>
Abstract
Plant photoreceptor phytochromes are phosphoproteins, but the question as to the functional role of phytochrome phosphorylation has remained to be elucidated. We investigated the functional role of phytochrome phosphorylation in plant light signaling using a Pfr-specific phosphorylation site mutant, Ser598Ala of oat (Avena sativa) phytochrome A (phyA). The transgenic Arabidopsis thaliana (phyA-201 background) plants with this mutant phyA showed hypersensitivity to light, suggesting that phytochrome phosphorylation at Serine-598 (Ser598) in the hinge region is involved in an inhibitory mechanism. The phosphorylation at Ser598 prevented its interaction with putative signal transducers, Nucleoside Diphosphate Kinase-2 and Phytochrome-Interacting Factor-3. These results suggest that phosphorylation in the hinge region of phytochromes serves as a signal-modulating site through the protein–protein interaction between phytochrome and its putative signal transducer proteins.
Acknowledgments
This work was supported by Korea Kumho Petrochemical (publication number 68) and in part by grants from the National Research Laboratory/Korea Institute of Science and Technology Evaluation and Planning, BioGreen 21 program of the Rural Development Administration (to P.-S.S.), the Crop Functional Genomics Center of the 21st Century Frontier Research Program by the Ministry of Science and Technology and the Rural Development Administration (code M101KG010001-03K0701-02910), and the Korea Science and Engineering Foundation/Ministry of Science and Technology to the Environmental Biotechnology National Core Research Center (to J.-I.K. and P.-S.S; Grant R15-2003-012-01003-0). We thank Veniamin N. Lapko for unpublished data and discussion. We also thank Andras Viczian for the cloning of the phytochrome-GFP constructs and the production of the phytochrome-GFP transgenic plants.
Notes
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