Abstract

Iron (Fe) is an essential nutrient for virtually all organisms, where it functions in critical electron transfer processes, like those involved in respiration. Photosynthetic organisms have special requirements for Fe due to its importance in photosynthesis. While the importance of Fe for mitochondria- and chloroplast-localized processes is clear, our understanding of the molecular mechanisms that underlie the trafficking of Fe to these compartments is not complete. Here, we describe the Arabidopsis mitochondrial iron transporters, MIT1 and MIT2, that belong to the mitochondrial carrier family (MCF) of transport proteins. MIT1 and MIT2 display considerable homology with known mitochondrial Fe transporters of other organisms. Expression of MIT1 or MIT2 rescues the phenotype of the yeast mrs3mrs4 mutant, which is defective in mitochondrial iron transport. Although the Arabidopsis mit1 and mit2 single mutants do not show any significant visible phenotypes, the double mutant mit1mit2 displays embryo lethality. Analysis of a mit1 −− /mit2 + − line revealed that MIT1 and MIT2 are essential for iron acquisition by mitochondria and proper mitochondrial function. In addition, loss of MIT function results in mislocalization of Fe, which in turn causes upregulation of the root high affinity Fe uptake pathway. Thus, MIT1 and MIT2 are required for the maintenance of both mitochondrial and whole plant Fe homeostasis, which, in turn, is important for the proper growth and development of the plant.

Highlights

  • Iron (Fe) is an essential element that is required for numerous biochemical processes in cells

  • We report the characterization of previously unidentified mitochondrial iron transporters in dicots for the first time

  • The H222 in MRS3 is conserved in MIT2, is replaced by another potential Fe-ligand, a tyrosine, in MIT1

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Summary

Introduction

Iron (Fe) is an essential element that is required for numerous biochemical processes in cells. Studies in rice and barley have shown that in response to iron limitation, phytosiderophores (PSs) are exported by transporter of mugineic acid (TOM1) and Fe-PS complexes are subsequently imported by YS1, a member of the oligopeptide transporter family (Curie et al, 2001; Inoue et al, 2009; Nozoye et al, 2011; Connorton et al, 2017). Dicots such as Arabidopsis, on the other

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