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The ferroxidases LPR1 and LPR2 control iron translocation in the xylem of Arabidopsis plants

Enzyme-catalyzed oxidation of Fe(II) to Fe(III) is necessary for maintaining the mobility of Fe translocation in the xylem.
Iron (Fe) deficiency is common in agricultural crops and affects millions of people worldwide. Translocation of Fe in the xylem is a key step for Fe accumulation in the above-ground parts of plants. It is well known that Fe is translocated as Fe(III)-citrate/malate complexes in the xylem. However, autooxidation of Fe(II) to Fe(III) is slow in the acidic environment of xylem sap, and Fe(III)-citrate/malate complexes formed in the xylem sap are easily photoreduced and unstable under light. Here, we show that two Arabidopsis ferroxidases, LPR1 and LPR2, are required to oxidize Fe(II) and maintain Fe(III)-citrate/malate stability and mobility during xylem translocation. LPR1 and LPR2 are mainly localized in the cell walls of xylem vessels. Knockout of both LPR1 and LPR2 increases the proportion of Fe(II) in the xylem sap, and causes Fe deposition along the vascular bundles especially in the petioles and main veins of leaves. Blocking blue light or decreasing light intensity alleviates Fe deposition along the xylem in the double mutant. The double mutant displays constitutive expression of Fe-deficiency response genes and overaccumulation of Fe in the roots and mature leaves under Fe-sufficient supply, but shows Fe-deficiency chlorosis in the new leaves and inflorescences under low Fe supply, as well as decreased Fe concentration in the seeds. The translocation of 57Fe along the xylem is impaired in the double mutant. Our study uncovers an essential physiological role of LPR1 and LPR2 and also reveals a new mechanism by which plants maintain Fe mobility during long-distance translocation in the xylem.
Read more: https://doi.org/10.1016/j.molp.2022.11.003
Contact: Fang-Jie Zhao (Fangjie.zhao@njau.edu.cn)
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