Structural insight into PIF6-mediated red light signal transduction of plant phytochrome B

Abstract 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 re...

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Main Authors: Hanli Jia, Zeyuan Guan, Junya Ding, Xiaoyu Wang, Dingfang Tian, Yan Zhu, Delin Zhang, Zhu Liu, Ling Ma, Ping Yin
Format: Article
Language:English
Published: Nature Publishing Group 2025-05-01
Series:Cell Discovery
Online Access:https://doi.org/10.1038/s41421-025-00802-3
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author Hanli Jia
Zeyuan Guan
Junya Ding
Xiaoyu Wang
Dingfang Tian
Yan Zhu
Delin Zhang
Zhu Liu
Ling Ma
Ping Yin
author_facet Hanli Jia
Zeyuan Guan
Junya Ding
Xiaoyu Wang
Dingfang Tian
Yan Zhu
Delin Zhang
Zhu Liu
Ling Ma
Ping Yin
author_sort Hanli Jia
collection DOAJ
description Abstract 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 phyBY276H‒PIF6 complex, and the truncated phyBNY276H‒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.
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spelling doaj-art-1eabd45555984de2baa53ac82bb80cff2025-08-20T03:08:40ZengNature Publishing GroupCell Discovery2056-59682025-05-0111111310.1038/s41421-025-00802-3Structural insight into PIF6-mediated red light signal transduction of plant phytochrome BHanli Jia0Zeyuan Guan1Junya Ding2Xiaoyu Wang3Dingfang Tian4Yan Zhu5Delin Zhang6Zhu Liu7Ling Ma8Ping Yin9National Key Laboratory of Crop Genetic Improvement, Hubei Hongshan Laboratory, Huazhong Agricultural UniversityNational Key Laboratory of Crop Genetic Improvement, Hubei Hongshan Laboratory, Huazhong Agricultural UniversityNational Key Laboratory of Crop Genetic Improvement, Hubei Hongshan Laboratory, Huazhong Agricultural UniversityNational Key Laboratory of Crop Genetic Improvement, Hubei Hongshan Laboratory, Huazhong Agricultural UniversityNational Key Laboratory of Crop Genetic Improvement, Hubei Hongshan Laboratory, Huazhong Agricultural UniversityNational Key Laboratory of Crop Genetic Improvement, Hubei Hongshan Laboratory, Huazhong Agricultural UniversityNational Key Laboratory of Crop Genetic Improvement, Hubei Hongshan Laboratory, Huazhong Agricultural UniversityNational Key Laboratory of Crop Genetic Improvement, Hubei Hongshan Laboratory, Huazhong Agricultural UniversityNational Key Laboratory of Crop Genetic Improvement, Hubei Hongshan Laboratory, Huazhong Agricultural UniversityNational Key Laboratory of Crop Genetic Improvement, Hubei Hongshan Laboratory, Huazhong Agricultural UniversityAbstract 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 phyBY276H‒PIF6 complex, and the truncated phyBNY276H‒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.https://doi.org/10.1038/s41421-025-00802-3
spellingShingle Hanli Jia
Zeyuan Guan
Junya Ding
Xiaoyu Wang
Dingfang Tian
Yan Zhu
Delin Zhang
Zhu Liu
Ling Ma
Ping Yin
Structural insight into PIF6-mediated red light signal transduction of plant phytochrome B
Cell Discovery
title Structural insight into PIF6-mediated red light signal transduction of plant phytochrome B
title_full Structural insight into PIF6-mediated red light signal transduction of plant phytochrome B
title_fullStr Structural insight into PIF6-mediated red light signal transduction of plant phytochrome B
title_full_unstemmed Structural insight into PIF6-mediated red light signal transduction of plant phytochrome B
title_short Structural insight into PIF6-mediated red light signal transduction of plant phytochrome B
title_sort structural insight into pif6 mediated red light signal transduction of plant phytochrome b
url https://doi.org/10.1038/s41421-025-00802-3
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