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A Phytochrome-Associated Protein Phosphatase 2A Modulates Light Signals in Flowering Time Control in Arabidopsis

^a Kumho Life and Environmental Science Laboratory, 1 Oryong-dong, Buk-gu, Kwangju 500-712, Korea
^b Department of Chemistry, University of Nebraska, Lincoln, Nebraska 68588

³ To whom correspondence should be addressed. E-mail pssong{at}kkpc.com or cmpark{at}snu.ac.kr; fax 82-2-889-1568

Reversible protein phosphorylation, which is catalyzed by functionally coupled protein kinases and protein phosphatases, is a major signaling mechanism in eukaryotic cellular functions. The red and far-red light–absorbing phytochrome photoreceptors are light-regulated Ser/Thr-specific protein kinases that regulate diverse photomorphogenic processes in plants. Here, we demonstrate that the phytochromes functionally interact with the catalytic subunit of a Ser/Thr-specific protein phosphatase 2A designated FyPP. The interactions were influenced by phosphorylation status and spectral conformation of the phytochromes. Recombinant FyPP efficiently dephosphorylated oat phytochrome A in the presence of Fe²⁺ or Zn²⁺ in a spectral form–dependent manner. FyPP was expressed predominantly in floral organs. Transgenic Arabidopsis plants with overexpressed or suppressed FyPP levels exhibited delayed or accelerated flowering, respectively, indicating that FyPP modulates phytochrome-mediated light signals in the timing of flowering. Accordingly, expression patterns of the clock genes in the long-day flowering pathway were altered greatly. These results indicate that a self-regulatory phytochrome kinase-phosphatase coupling is a key signaling component in the photoperiodic control of flowering.

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