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Author Zhou J., Hu Q., Xiao X., Yao D., Ge S., Ye J., Li H., Cai R., Liu R., Meng F., Wang C., Zhu J.K., Lei M., Xing W.
Title Mechanism of phosphate sensing and signaling revealed by rice SPX1-PHR2 complex structure.
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 alpha1 can impose a steric hindrance when interacting with the PHR2 dimer. By stabilizing helix alpha1, 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.
Journal Nat Commun
Country China
Volume 12(1)
Pages 7040
Year 2021
PubMed ID 34857773
PubMed Central ID 8639918
DOI 10.1038/s41467-021-27391-5
URL -
Relation
Gene PHR2 SPX1
INSD -
Strain Wild Core Collection -
Induced Mutation Lines(NIG Collection) -
Sterile Seed Strain -
Lethal Embryo
Mutantion Strain
-
Stages in Each Organ
- Muant Lines (Gene)
-
Cultivated Varieties(NIG Collection) -
Stages in Each Organ -
/rice/oryzabase