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Differential phosphorylation of the N - terminal extension regulates phytochrome B signaling

Colaborador(es): Viczián, András. Institute of Plant Biology. Biological Research Centre. Szeged, Hungary | Ádám, Éva. Institute of Plant Biology. Biological Research Centre. Szeged, Hungary. University of Szeged. Department of Dermatology and Allergology. Institute of Translational Biomedicine. Szeged, Hungary | Staudt, Anne Marie. University of Freiburg. Institute of Biology II. Freiburg, Germany | Lambert, Dorothee. University of Freiburg. Institute of Biology II. Freiburg, Germany | Klement, Eva. Biological Research Centre. Laboratory of Proteomics Research. Szeged, Hungary | Romero Montepaone, Sofía. Universidad de Buenos Aires. Facultad de Agronomía. Instituto de Investigaciones Fisiológicas y Ecológicas Vinculadas a la Agricultura (IFEVA). Buenos Aires, Argentina. CONICET – Universidad de Buenos Aires. Instituto de Investigaciones Fisiológicas y Ecológicas Vinculadas a la Agricultura (IFEVA). Buenos Aires, Argentina | Hiltbrunner, Andreas. University of Freiburg. Institute of Biology II. Freiburg, Germany. University of Freiburg. Signalling Research Centres BIOSS and CIBSS. Freiburg, Germany | Casal, Jorge José. Universidad de Buenos Aires. Facultad de Agronomía. Instituto de Investigaciones Fisiológicas y Ecológicas Vinculadas a la Agricultura (IFEVA). Buenos Aires, Argentina. CONICET – Universidad de Buenos Aires. Instituto de Investigaciones Fisiológicas y Ecológicas Vinculadas a la Agricultura (IFEVA). Buenos Aires, Argentina. CONICET. Fundación Instituto Leloir. Buenos Aires, Argentina.
ISSN: 0028-646X.Tipo de material: Artículos y capítulos. Recurso electrónico.Tema(s): | DARK REVERSION | PHOSPHORYLATION | PHYB NTE | PHYTOCHROME | THERMAL REVERSION | Recursos en línea: Haga clic para acceso en línea | LINK AL EDITOR En: New phytologist Vol.225, no.5 (2020), p.1635–1650, grafs.Resumen: Phytochrome B (phyB) is an excellent light quality and quantity sensor that can detect subtle changes in the light environment. The relative amounts of the biologically active photoreceptor (phyB Pfr) are determined by the light conditions and light independent thermal relaxation of Pfr into the inactive phyB Pr, termed thermal reversion. Little is known about the regulation of thermal reversion and how it affects plants’ light sensitivity. In this study we identified several serine/threonine residues on the N-terminal extension (NTE) of Arabidopsis thaliana phyB that are differentially phosphorylated in response to light and temperature, and examined transgenic plants expressing nonphosphorylatable and phosphomimic phyB mutants. The NTE of phyB is essential for thermal stability of the Pfr form, and phosphorylation of S86 particularly enhances the thermal reversion rate of the phyB Pfr–Pr heterodimer in vivo. We demonstrate that S86 phosphorylation is especially critical for phyB signaling compared with phosphorylation of the more N terminal residues. Interestingly, S86 phosphorylation is reduced in light, paralleled by a progressive Pfr stabilization under prolonged irradiation. By investigating other phytochromes (phyD and phyE) we provide evidence that acceleration of thermal reversion by phosphorylation represents a general mechanism for attenuating phytochrome signaling.
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Phytochrome B (phyB) is an excellent light quality and quantity sensor that can detect subtle changes in the light environment. The relative amounts of the biologically active photoreceptor (phyB Pfr) are determined by the light conditions and light independent thermal relaxation of Pfr into the inactive phyB Pr, termed thermal reversion. Little is known about the regulation of thermal reversion and how it affects plants’ light sensitivity.
In this study we identified several serine/threonine residues on the N-terminal extension (NTE) of Arabidopsis thaliana phyB that are differentially phosphorylated in response to light and temperature, and examined transgenic plants expressing nonphosphorylatable and phosphomimic phyB mutants.
The NTE of phyB is essential for thermal stability of the Pfr form, and phosphorylation of S86 particularly enhances the thermal reversion rate of the phyB Pfr–Pr heterodimer in vivo. We demonstrate that S86 phosphorylation is especially critical for phyB signaling compared with phosphorylation of the more N terminal residues. Interestingly, S86 phosphorylation is reduced in light, paralleled by a progressive Pfr stabilization under prolonged irradiation.
By investigating other phytochromes (phyD and phyE) we provide evidence that acceleration of thermal reversion by phosphorylation represents a general mechanism for attenuating phytochrome signaling.

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