{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Guan Z"],"funding":["European Research Council"],"pagination":["1581"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8948245"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["13(1)"],"pubmed_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/InsP<sub>6</sub>/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/InsP<sub>6</sub>/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 inactiva"],"journal":["Nature communications"],"pubmed_title":["Mechanistic insights into the regulation of plant phosphate homeostasis by the rice SPX2 - PHR2 complex."],"pmcid":["PMC8948245"],"funding_grant_id":["818696"],"pubmed_authors":["Zhang D","Yan J","Hothorn M","Chen J","Pei K","Liu R","Zhang Q","Liu Z","Guan Z","Wang Q","Zhang Z","Zuo J","Cheng P","Savarin J","Broger L","Yin P","Zou T"],"additional_accession":[]},"is_claimable":false,"name":"Mechanistic insights into the regulation of plant phosphate homeostasis by the rice SPX2 - PHR2 complex.","description":"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/InsP<sub>6</sub>/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/InsP<sub>6</sub>/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 inactiva","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Mar","modification":"2026-06-01T03:05:40.285Z","creation":"2024-11-20T08:53:25.779Z"},"accession":"S-EPMC8948245","cross_references":{"pubmed":["35332155"],"doi":["10.1038/s41467-022-29275-8"]}}