Residues Clustered in the Light-Sensing Knot of Phytochrome B are Necessary for Conformer-Specific Binding to Signaling Partner PIF3
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- Oka Yoshito
- UC Berkeley/PGEC Grad. Sch. of Sci., Kyoto Univ.
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- Kikis Elise
- UC Berkeley/PGEC
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- Hudson Matthew
- National Soybean Research Center
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- Nagatani Akira
- Grad. Sch. of Sci., Kyoto Univ.
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- Quail Peter
- UC Berkeley/PGEC
Bibliographic Information
- Other Title
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- Phytochrome BのN末端領域内の結び目構造はPIF3との相互作用に関わる
Abstract
PHYTOCHROME INTERACTING FACTOR 3 (PIF3) interacts with the active phytochrome B (phyB). To identify mutations in the phyB N-terminus that disrupt this interaction, we developed a yeast reverse-hybrid screen. Fifteen mutations identified in this screen, or in previous genetic screens for Arabidopsis mutants showing reduced sensitivity to red light, were shown to disrupt light-induced binding of phyB to PIF3 in in vitro binding assays. These phyB mutations fall into two classes: Class I (11 mutations) containing those defective in light perception, and Class II (4 mutations) containing those normal in light perception, but defective in binding to PIF3. A bioinformatics comparison of phyB to BphP, for which a crystal structure has been solved, predicts that three of the four Class II mutated residues are solvent exposed in a cleft between PAS and GAF domains, suggesting that these residues could be directly required for the physical interaction of phyB with PIF3.
Journal
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- Plant and Cell Physiology Supplement
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Plant and Cell Physiology Supplement 2009 (0), 0288-0288, 2009
The Japanese Society of Plant Physiologists
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Details 詳細情報について
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- CRID
- 1390001205632530560
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- NII Article ID
- 130006994270
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- Data Source
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- JaLC
- CiNii Articles
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- Abstract License Flag
- Disallowed