Mechanistic insights into the regulation of plant phosphate homeostasis by the rice SPX2 – PHR2 complex

Zeyuan Guan, Qunxia Zhang, Zhifei Zhang, Jiaqi Zuo, Juan Chen, Ruiwen Liu, Julie Savarin, Larissa Broger, Peng Cheng, Qiang Wang, Kai Pei, Delin Zhang, Tingting Zou, Junjie Yan, Ping Yin, Michael Hothorn and Zhu Liu ()
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Zeyuan Guan: Huazhong Agricultural University
Qunxia Zhang: Huazhong Agricultural University
Zhifei Zhang: Huazhong Agricultural University
Jiaqi Zuo: Huazhong Agricultural University
Juan Chen: Huazhong Agricultural University
Ruiwen Liu: Huazhong Agricultural University
Julie Savarin: University of Geneva
Larissa Broger: University of Geneva
Peng Cheng: Huazhong Agricultural University
Qiang Wang: Huazhong Agricultural University
Kai Pei: Huazhong Agricultural University
Delin Zhang: Huazhong Agricultural University
Tingting Zou: Huazhong Agricultural University
Junjie Yan: Huazhong Agricultural University
Ping Yin: Huazhong Agricultural University
Michael Hothorn: University of Geneva
Zhu Liu: Huazhong Agricultural University

Nature Communications, 2022, vol. 13, issue 1, 1-10

Abstract: Abstract Phosphate (Pi) starvation response (PHR) transcription factors play key roles in plant Pi homeostasis maintenance. They are negatively regulated by stand-alone SPX proteins, cellular receptors for inositol pyrophosphate (PP-InsP) nutrient messengers. How PP-InsP-bound SPX interacts with PHRs is poorly understood. Here, we report crystal structures of the rice SPX2/InsP6/PHR2 complex and of the PHR2 DNA binding (MYB) domain in complex with target DNA at resolutions of 3.1 Å and 2.7 Å, respectively. In the SPX2/InsP6/PHR2 complex, the signalling-active SPX2 assembles into a domain-swapped dimer conformation and binds two copies of PHR2, targeting both its coiled-coil (CC) oligomerisation domain and MYB domain. Our results reveal that the SPX2 senses PP-InsPs to inactivate PHR2 by establishing severe steric clashes with the PHR2 MYB domain, preventing DNA binding, and by disrupting oligomerisation of the PHR2 CC domain, attenuating promoter binding. Our findings rationalize how PP-InsPs activate SPX receptor proteins to target PHR family transcription factors.

Date: 2022
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-29275-8

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DOI: 10.1038/s41467-022-29275-8

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