Iron uptake, trafficking and homeostasis in plants.

Iron is an essential micronutrient with numerous cellular functions, and its deficiency represents one of the most serious problems in human nutrition worldwide. Plants have two major problems with iron as a free ion: its insolubility and its toxicity. To ensure iron acquisition from soil and to avoid iron excess in the cells, uptake and homeostasis are tightly controlled. Plants meet the extreme insolubility of oxidized iron at neutral pH values by deficiency-inducible chelation and reduction systems at the root surface that facilitate uptake. Inside the cells the generation of highly toxic hydroxyl radicals by iron redox changes is avoided by intricate chelation mechanisms. Organic acids, most notably nicotianamine, and specialized proteins bind iron before it can be inserted into target molecules for biological function. Uptake and trafficking of iron throughout the plant is therefore a highly integrated process of membrane transport and reduction, trafficking between chelator species, whole-plant allocation and genetic regulation. The improvement of crop plants with respect to iron efficiency on iron-limiting soils and to iron fortification for human nutrition has been initiated by breeding and biotechnology. These efforts have to consider molecular and physiological evidence to overcome the inherent barriers and problems of iron metabolism.

Post-translational modifications of the AFET3 gene product: a component of the iron transport system in budding cells and mycelia of the yeast Arxula adeninivorans.

The yeast Arxula adeninivorans is characterized by a temperature-dependent dimorphism. A. adeninivorans grows as budding cells at temperatures up to 42 degrees C, but forms mycelia at higher temperatures. A strong correlation exists between morphological status and iron uptake, achieved by two transport systems that differ in iron affinity. In the presence of high Fe(II) concentrations (>2 microm), budding cells accumulate iron concentrations up to seven-fold higher than those observed in mycelia, while at low Fe(II) concentrations (<2 microm), both cell types accumulate similar amounts of iron. The copper-dependent Fe(II) oxidase Afet3p, composed of 615 amino acids, is a component of the high-affinity iron transport system. This protein shares a high degree of homology with other yeast iron transport proteins, namely Fet3p of Saccharomyces cerevisiae, Cafet3p of Candida albicans and Pfet3p of Pichia pastoris. Expression of the AFET3 gene is found to be strongly dependent on iron concentration but independent of the morphological stage; however, cell morphology was found to influence post-translational modifications of the gene product. O-glycosylation was observed in budding cells only, whereas N-glycosylation occurred in both cell types. The N-glycosylated 103 kDa glycoprotein matures into the 108.5 kDa form, further characterized by serine phosphorylation. Both N-glycosylation and phosphorylation occur at low iron concentrations (< or =5 microm). The mature Afet3p of 108.5 kDa is uniformly distributed within the plasma membrane in cells of both morphological stages.

A metal-binding member of the late embryogenesis abundant protein family transports iron in the phloem of Ricinus communis L.

The transport of metal micronutrients to developing organs in a plant is mediated primarily by the sieve elements. Ligands are thought to form complexes with the free ions in order to prevent cellular damage, but no binding partners have been unequivocally identified from plants so far. This study has used the phloem-mediated transport of micronutrients during the germination of the castor bean seedling to identify an iron transport protein (ITP). It is demonstrated that essentially all (55)Fe fed to seedlings is associated with the protein fraction of phloem exudate. It is shown that ITP carries iron in vivo and binds additional iron in vitro. ITP was purified to homogeneity from minute amounts of phloem exudate using immobilized metal ion affinity chromatography. It preferentially binds to Fe(3+) but not to Fe(2+) and also complexes Cu(2+), Zn(2+), and Mn(2+) in vitro. The corresponding cDNA of ITP was cloned using internal peptide fragments. The deduced protein of 96 amino acids shows high similarity to the stress-related family of late embryogenesis abundant proteins. Its predicted characteristics and its RNA expression pattern are consistent with a function in metal ion binding. The ITP from Ricinus provides the first identified micronutrient binding partner for phloem-mediated long distance transport in plants and is the first member of the late embryogenesis abundant protein family shown to have such a function.