Whitfield, Hayley L., Gilmartin, Megan, Riley, Andrew M., Shipton, Megan L., Potter, Barry V. L., Hemmings, Andrew M and Brearley, Charles A. (2026) The intracellular inositol (pyro)phosphate receptor AtSPX1 reciprocally binds to P1BS DNA. Nature Communications. ISSN 2041-1723
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Abstract
The response of plants to phosphate starvation engages PHR (CC-MYB-PHOSPHATE STARVATION RESPONSE) transcription factors that bind to P1BS (GNATATNC) promoter elements of phosphate-starvation induced (PSI) genes. The encoded proteins include single-domain SPX (SYG1/Pho81/XPR1) proteins. SPX proteins bind PHR proteins. Current models of SPX1: PHR interaction define only a high-phosphate role for SPX1, as an inositol (pyro)phosphate-dependent negative regulator of PHR. Here, by combination of chemical synthesis, orthogonal binding assays and molecular modeling we report that full-length SPX1 binds P1BS promoter elements and inositol (pyro)phosphates with similar affinity. Inositol (pyro)phosphates and DNA are reciprocally competing ligands of SPX1. Structural models of SPX1: inositol (pyrophosphate) and of SPX1: P1BS interaction are provided beside a working hypothesis of SPX1: PHR1 interaction. The results reveal the low-phosphate function of SPX1. These findings proffer a fundamentally different perspective of SPX involvement in the phosphate starvation response (PSR).
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | abiotic,plant physiology,proteins |
| Faculty \ School: | Faculty of Science > School of Biological Sciences |
| UEA Research Groups: | Faculty of Science > Research Groups > Plant Sciences Faculty of Science > Research Groups > Molecular Microbiology |
| Related URLs: | |
| Depositing User: | LivePure Connector |
| Date Deposited: | 09 Mar 2026 16:31 |
| Last Modified: | 15 Mar 2026 06:30 |
| URI: | https://ueaeprints.uea.ac.uk/id/eprint/102276 |
| DOI: | 10.1038/s41467-026-69810-5 |
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