{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["32(10)"],"submitter":["Naumann C"],"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<sub>M</sub> ∼ 2 μM Fe<sup>2+</sup>). LPR1 typifies an ancient, Fe-oxidizing multicopper protein family that evolved early upon bacterial land colonizat"],"journal":["Current biology : CB"],"pagination":["2189-2205.e6"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9168544"],"repository":["biostudies-literature"],"pubmed_title":["Bacterial-type ferroxidase tunes iron-dependent phosphate sensing during Arabidopsis root development."],"pmcid":["PMC9168544"],"pubmed_authors":["Heisters M","Quint M","Abel S","Mechtler K","Imre R","Hoehenwarter W","Brandt W","Tang N","Naumann C","Janitza P","Ziegler J","Alfs C","Sawers G","Dagdas Y","Toto Nienguesso A"],"additional_accession":[]},"is_claimable":false,"name":"Bacterial-type ferroxidase tunes iron-dependent phosphate sensing during Arabidopsis root development.","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<sub>M</sub> ∼ 2 μM Fe<sup>2+</sup>). LPR1 typifies an ancient, Fe-oxidizing multicopper protein family that evolved early upon bacterial land colonizat","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 May","modification":"2026-05-09T23:46:09.904Z","creation":"2025-04-04T22:14:48.83Z"},"accession":"S-EPMC9168544","cross_references":{"pubmed":["35472311"],"doi":["10.1016/j.cub.2022.04.005"]}}