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-Structure paper
| タイトル | Structural insight into PIF6-mediated red light signal transduction of plant phytochrome B. |
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| ジャーナル・号・ページ | Cell Discov, Vol. 11, Issue 1, Page 51, Year 2025 |
| 掲載日 | 2025年5月22日 |
著者 | Hanli Jia / Zeyuan Guan / Junya Ding / Xiaoyu Wang / Dingfang Tian / Yan Zhu / Delin Zhang / Zhu Liu / Ling Ma / Ping Yin / ![]() |
| PubMed 要旨 | The red/far-red light receptor phytochrome B (phyB) plays essential roles in regulating various plant development processes. PhyB exists in two distinct photoreversible forms: the inactive Pr form ...The red/far-red light receptor phytochrome B (phyB) plays essential roles in regulating various plant development processes. PhyB exists in two distinct photoreversible forms: the inactive Pr form and the active Pfr form. phyB-Pfr binds phytochrome-interacting factors (PIFs) to transduce red light signals. Here, we determined the cryo-electron microscopy (cryo-EM) structures of the photoactivated phyB-Pfr‒PIF6 complex, the constitutively active mutant phyB‒PIF6 complex, and the truncated phyBN‒PIF6 complex. In these structures, two parallel phyB-Pfr molecules interact with one PIF6 molecule. Red light-triggered rotation of the PΦB D-ring leads to the conversion of hairpin loops into α helices and the "head-to-head" reassembly of phyB-Pfr N-terminal photosensory modules. The interaction between phyB-Pfr and PIF6 influences the dimerization and transcriptional activation activity of PIF6, and PIF6 stabilizes the N-terminal extension of phyB-Pfr and increases the Pr→Pfr photoconversion efficiency of phyB. Our findings reveal the molecular mechanisms underlying Pr→Pfr photoconversion and PIF6-mediated red light signal transduction of phyB. |
リンク | Cell Discov / PubMed:40404641 / PubMed Central |
| 手法 | EM (単粒子) |
| 解像度 | 2.8 - 3.0 Å |
| 構造データ | EMDB-60816, PDB-9irk: EMDB-60860, PDB-9itf: EMDB-61582, PDB-9jlb: |
| 化合物 | ![]() ChemComp-O6E: |
| 由来 |
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キーワード | GENE REGULATION / PIF6-mediated / red light / signal transduction / phytochrome B |
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