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