Details

Autor(en) / Beteiligte

• Naumann, Christin
• Heisters, Marcus
• Brandt, Wolfgang
• Janitza, Philipp
• Alfs, Carolin
• Tang, Nancy
• Toto Nienguesso, Alicia
• Ziegler, Jörg
• Imre, Richard
• Mechtler, Karl
• Dagdas, Yasin
• Hoehenwarter, Wolfgang
• Sawers, Gary
• Quint, Marcel
• Abel, Steffen

Titel

Bacterial-type ferroxidase tunes iron-dependent phosphate sensing during Arabidopsis root development

Ist Teil von

• Current biology, 2022-05, Vol.32 (10), p.2189-2205.e6

Ort / Verlag

England: Elsevier Inc

Erscheinungsjahr

2022

Link zum Volltext

Quelle

EZB Electronic Journals Library

Beschreibungen/Notizen

• 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 KM ∼ 2 μM Fe2+). LPR1 typifies an ancient, Fe-oxidizing multicopper protein family that evolved early upon bacterial land colonization. The ancestor of streptophyte algae and embryophytes (land plants) acquired LPR1-type ferroxidase from soil bacteria via horizontal gene transfer, a hypothesis supported by phylogenomics, homology modeling, and biochemistry. Our molecular and kinetic data on LPR1 regulation indicate that Pi-dependent Fe substrate availability determines LPR1 activity and function. Guided by the metabolic lifestyle of extant sister bacterial genera, we propose that Arabidopsis LPR1 monitors subtle concentration differentials of external Fe availability as a Pi-dependent cue to adjust root meristem maintenance via Fe redox signaling and cell wall modification. We further hypothesize that the acquisition of bacterial LPR1-type ferroxidase by embryophyte progenitors facilitated the evolution of local Pi sensing and acquisition during plant terrestrialization. [Display omitted] •Arabidopsis thaliana LPR1 multicopper oxidase typifies a novel ferroxidase cohort•Fe availability tunes LPR1-dependent root responses to phosphate (Pi) limitation•LPR1 specificity links Fe-Pi interactions to root Pi sensing via redox cycling•Streptophyte ancestors acquired LPR1-type ferroxidase from soil bacteria by HGT Phosphate (Pi) availability guides root growth. Naumann et al. show Arabidopsis LPR1 typifies a novel ferroxidase that links antagonistic Fe-Pi interactions to local Pi sensing by root tips via Fe redox cycling. Streptophyte ancestors gained LPR1-type ferroxidase from soil bacteria by horizontal gene transfer, which benefited plant terrestrialization.