Open AccessPhytochrome Phosphorylation Modulates Light Signaling by Influencing the Protein–Protein Interaction[W]
Author(s) -
JeongIl Kim,
Yu Shen,
YunJeong Han,
Joung-Eun Park,
Daniel Kirchenbauer,
MoonSoo Soh,
Ferenc Nagy,
Eberhard Schäfer,
PillSoon Song
Publication year - 2004
Publication title -
the plant cell
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.324
H-Index - 341
eISSN - 1532-298X
pISSN - 1040-4651
DOI - 10.1105/tpc.104.023879
Subject(s) - biology , phytochrome , phosphorylation , protein phosphorylation , microbiology and biotechnology , signal transduction , biophysics , botany , red light , protein kinase a
Plant photoreceptor phytochromes are phosphoproteins, but the question as to the functional role of phytochrome phosphorylation has remained to be elucidated. We investigated the functional role of phytochrome phosphorylation in plant light signaling using a Pfr-specific phosphorylation site mutant, Ser598Ala of oat (Avena sativa) phytochrome A (phyA). The transgenic Arabidopsis thaliana (phyA-201 background) plants with this mutant phyA showed hypersensitivity to light, suggesting that phytochrome phosphorylation at Serine-598 (Ser598) in the hinge region is involved in an inhibitory mechanism. The phosphorylation at Ser598 prevented its interaction with putative signal transducers, Nucleoside Diphosphate Kinase-2 and Phytochrome-Interacting Factor-3. These results suggest that phosphorylation in the hinge region of phytochromes serves as a signal-modulating site through the protein-protein interaction between phytochrome and its putative signal transducer proteins.
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