title: Phosphorylation of phytochrome B inhibits light-induced signaling via accelerated dark reversion in Arabidopsis.
abstract: The photoreceptor phytochrome B (phyB) interconverts between the biologically active Pfr (λmax = 730 nm) and inactive Pr (λmax = 660 nm) forms in a red/far-red-dependent fashion and regulates, as molecular switch, many aspects of light-dependent development in Arabidopsis thaliana. phyB signaling is launched by the biologically active Pfr conformer and mediated by specific protein-protein interactions between phyB Pfr and its downstream regulatory partners, whereas conversion of Pfr to Pr terminates signaling. Here, we provide evidence that phyB is phosphorylated in planta at Ser-86 located in the N-terminal domain of the photoreceptor. Analysis of phyB-9 transgenic plants expressing phospho-mimic and nonphosphorylatable phyB-yellow fluorescent protein (YFP) fusions demonstrated that phosphorylation of Ser-86 negatively regulates all physiological responses tested. The Ser86Asp and Ser86Ala substitutions do not affect stability, photoconversion, and spectral properties of the photoreceptor, but light-independent relaxation of the phyB(Ser86Asp) Pfr into Pr, also termed dark reversion, is strongly enhanced both in vivo and in vitro. Faster dark reversion attenuates red light-induced nuclear import and interaction of phyB(Ser86Asp)-YFP Pfr with the negative regulator PHYTOCHROME INTERACTING FACTOR3 compared with phyB-green fluorescent protein. These data suggest that accelerated inactivation of the photoreceptor phyB via phosphorylation of Ser-86 represents a new paradigm for modulating phytochrome-controlled signaling.
authors: Faculty of Biology, University of Freiburg, D-79104, Freiburg Germany.
authors: Mátyás
authors: M
authors: Medzihradszky
authors: János
authors: J
authors: Bindics
authors: Éva
authors: É
authors: Ádám
authors: András
authors: A
authors: Viczián
authors: Éva
authors: É
authors: Klement
authors: Séverine
authors: S
authors: Lorrain
authors: Péter
authors: P
authors: Gyula
authors: Zsuzsanna
authors: Z
authors: Mérai
authors: Christian
authors: C
authors: Fankhauser
authors: Katalin F
authors: KF
authors: Medzihradszky
authors: Tim
authors: T
authors: Kunkel
authors: Eberhard
authors: E
authors: Schäfer
authors: Ferenc
authors: F
authors: Nagy
mesh_terms: D017360:Arabidopsis / Q000502:physiology*; D029681:Arabidopsis Proteins / Q000235:genetics / Q000378:metabolism*; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism; D051792:Basic Helix-Loop-Helix Proteins / Q000235:genetics / Q000378:metabolism; D003624:Darkness; D008027:Light; D008164:Luminescent Proteins / Q000235:genetics / Q000378:metabolism; D010766:Phosphorylation; D051939:Phytochrome B / Q000235:genetics / Q000378:metabolism*; D030821:Plants, Genetically Modified / Q000378:metabolism; D055550:Protein Stability; D017434:Protein Structure, Tertiary; D036226:Seedlings / Q000235:genetics / Q000254:growth & development; D012694:Serine / Q000378:metabolism; D015398:Signal Transduction; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
chemical_list: D029681:Arabidopsis Proteins; D001426:Bacterial Proteins; D051792:Basic Helix-Loop-Helix Proteins; D008164:Luminescent Proteins; D051939:Phytochrome B; D012694:Serine; C497952:PHYB protein, Arabidopsis; C116162:PIF3 protein, Arabidopsis; C054562:yellow fluorescent protein, Bacteria
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