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Updated: May 2, 2026

Photoconversion of Purified Fluorescent Proteins and Dual-probe Optical Highlighting in Live Cells
Published on: June 27, 2010
Photoconversion and nuclear trafficking cycles determine phytochrome A's response profile to far-red light
Julia Rausenberger1, Anke Tscheuschler, Wiebke Nordmeier
1Centre for Biological Systems Analysis (ZBSA), University of Freiburg, 79104 Freiburg, Germany.
Abstract:
Phytochrome A (phyA) is the only photoreceptor in plants, initiating responses in far-red light and, as such, essential for survival in canopy shade. Although the absorption and the ratio of active versus total phyA are maximal in red light, far-red light is the most efficient trigger of phyA-dependent responses. Using a joint experimental-theoretical approach, we unravel the mechanism underlying this shift of the phyA action peak from red to far-red light and show that it relies on specific molecular interactions rather than on intrinsic changes to phyA's spectral properties. According to our model, the dissociation rate of the phyA-FHY1/FHL nuclear import complex is a principle determinant of the phyA action peak. The findings suggest how higher plants acquired the ability to sense far-red light from an ancestral photoreceptor tuned to respond to red light.
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