Mechanism of phosphate sensing and signaling revealed by rice SPX1-PHR2 complex structure

Jia Zhou, Qinli Hu, Xinlong Xiao, Deqiang Yao, Shenghong Ge, Jin Ye, Haojie Li, Rujie Cai, Renyang Liu, Fangang Meng, Chao Wang, Jian-Kang Zhu, Mingguang Lei () and Weiman Xing ()
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Jia Zhou: Chinese Academy of Sciences
Qinli Hu: Chinese Academy of Sciences
Xinlong Xiao: Chinese Academy of Sciences
Deqiang Yao: Shanghai Jiao Tong University School of Medicine
Shenghong Ge: Chinese Academy of Sciences
Jin Ye: University of Science and Technology of China
Haojie Li: Chinese Academy of Sciences
Rujie Cai: Shanghai Normal University
Renyang Liu: Chinese Academy of Sciences
Fangang Meng: Capital Medical University
Chao Wang: University of Science and Technology of China
Jian-Kang Zhu: Chinese Academy of Sciences
Mingguang Lei: Chinese Academy of Sciences
Weiman Xing: Shanghai Normal University

Nature Communications, 2021, vol. 12, issue 1, 1-10

Abstract: Abstract Phosphate, a key plant nutrient, is perceived through inositol polyphosphates (InsPs) by SPX domain-containing proteins. SPX1 an inhibit the PHR2 transcription factor to maintain Pi homeostasis. How SPX1 recognizes an InsP molecule and represses transcription activation by PHR2 remains unclear. Here we show that, upon binding InsP6, SPX1 can disrupt PHR2 dimers and form a 1:1 SPX1-PHR2 complex. The complex structure reveals that SPX1 helix α1 can impose a steric hindrance when interacting with the PHR2 dimer. By stabilizing helix α1, InsP6 allosterically decouples the PHR2 dimer and stabilizes the SPX1-PHR2 interaction. In doing so, InsP6 further allows SPX1 to engage with the PHR2 MYB domain and sterically block its interaction with DNA. Taken together, our results suggest that, upon sensing the surrogate signals of phosphate, SPX1 inhibits PHR2 via a dual mechanism that attenuates dimerization and DNA binding activities of PHR2.

Date: 2021
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DOI: 10.1038/s41467-021-27391-5

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