<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>32(10)</volume><submitter>Naumann C</submitter><pubmed_abstract>Access to inorganic phosphate (Pi), a principal intermediate of energy and nucleotide metabolism, profoundly affects cellular activities and plant performance. In most soils, antagonistic Pi-metal interactions restrict Pi bioavailability, which guides local root development to maximize Pi interception. Growing root tips scout the essential but immobile mineral nutrient; however, the mechanisms monitoring external Pi status are unknown. Here, we show that Arabidopsis LOW PHOSPHATE ROOT 1 (LPR1), one key determinant of Fe-dependent Pi sensing in root meristems, encodes a novel ferroxidase of high substrate specificity and affinity (apparent K&lt;sub>M&lt;/sub> ∼ 2 μM Fe&lt;sup>2+&lt;/sup>). LPR1 typifies an ancient, Fe-oxidizing multicopper protein family that evolved early upon bacterial land colonizat</pubmed_abstract><journal>Current biology : CB</journal><pagination>2189-2205.e6</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9168544</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Bacterial-type ferroxidase tunes iron-dependent phosphate sensing during Arabidopsis root development.</pubmed_title><pmcid>PMC9168544</pmcid><pubmed_authors>Heisters M</pubmed_authors><pubmed_authors>Quint M</pubmed_authors><pubmed_authors>Abel S</pubmed_authors><pubmed_authors>Mechtler K</pubmed_authors><pubmed_authors>Imre R</pubmed_authors><pubmed_authors>Hoehenwarter W</pubmed_authors><pubmed_authors>Brandt W</pubmed_authors><pubmed_authors>Tang N</pubmed_authors><pubmed_authors>Naumann C</pubmed_authors><pubmed_authors>Janitza P</pubmed_authors><pubmed_authors>Ziegler J</pubmed_authors><pubmed_authors>Alfs C</pubmed_authors><pubmed_authors>Sawers G</pubmed_authors><pubmed_authors>Dagdas Y</pubmed_authors><pubmed_authors>Toto Nienguesso A</pubmed_authors></additional><is_claimable>false</is_claimable><name>Bacterial-type ferroxidase tunes iron-dependent phosphate sensing during Arabidopsis root development.</name><description>Access to inorganic phosphate (Pi), a principal intermediate of energy and nucleotide metabolism, profoundly affects cellular activities and plant performance. In most soils, antagonistic Pi-metal interactions restrict Pi bioavailability, which guides local root development to maximize Pi interception. Growing root tips scout the essential but immobile mineral nutrient; however, the mechanisms monitoring external Pi status are unknown. Here, we show that Arabidopsis LOW PHOSPHATE ROOT 1 (LPR1), one key determinant of Fe-dependent Pi sensing in root meristems, encodes a novel ferroxidase of high substrate specificity and affinity (apparent K&lt;sub>M&lt;/sub> ∼ 2 μM Fe&lt;sup>2+&lt;/sup>). LPR1 typifies an ancient, Fe-oxidizing multicopper protein family that evolved early upon bacterial land colonizat</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022 May</publication><modification>2026-05-09T23:46:09.904Z</modification><creation>2025-04-04T22:14:48.83Z</creation></dates><accession>S-EPMC9168544</accession><cross_references><pubmed>35472311</pubmed><doi>10.1016/j.cub.2022.04.005</doi></cross_references></HashMap>