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Light regulation of phytochrome functions.

A, light-regulated His kinase activity


initiates phytochrome-mediated light signaling in prokaryotes. The cyanobacterial
phytochrome
1
(Cph1)
has
light-modulated
protein
kinase
activity.
Autophosphorylation is attenuated by red light and increased by far-red light.
Phosphorylated Pr could trigger a light signal. The phosphorylated Pr transfers its
phosphate to the Rcp response regulator; this could in turn initiate light signaling.
Phosphorylated Rcp could transfer this phosphate to a yet to be determined
acceptor (X). Note that for most plant phytochrome responses Pfr is the active
isoform. B,nuclear events in plant phytochrome signaling. Phytochrome B only
translocates into the nucleus in its far-red light absorbing form (PfrB). In the nucleus
PfrB interacts with the DNA-bound PIF3 transcription factor. Phytochrome A
translocates into the nucleus in its red light absorbing form, Pr* (Pr that has been
cycled through Pfr; this occurs preferentially in far-red rich light). Translocation also
occurs for Pfr (the far-red absorbing form); however, irradiation of plants with red
light triggers rapid phyA degradation. In the nucleus phyA presumably affects RSF1mediated gene activation. PKS1 is a negative regulator of phytochrome signaling; it
has been proposed that PKS1 inhibits nuclear translocation of phytochromes. C,
other light-regulated properties of plant phytochrome. Light affects the Ser/Thr
protein kinase activity of phytochromes. Contrary to Cph1, oat phyA has higher
auto- and trans-phosphorylation activity in the Pfr form. Interaction with signaling
intermediates is also isoform-dependent; this is true for PIF3, which is nuclear, and
for NDPK2, which is found both in the nucleus and the cytoplasm. The protein
stability of phyA is very much reduced in its far-red absorbing form (Pfr).