, Volume 31, Issue 1, pp 19-48

Structure and function of metal chelators produced by plants

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Abstract

Plants produce a range of ligands for cadmium (Cd), copper (Cu), nickel (Ni), and zinc (Zn). Cd- and Zn-citrate complexes are prevalent in leaves, even though malate is more abundant. In the xylem sap moving from roots to leaves, citrate and histidine are the principal ligands for Cu, Ni, and Zn. Phosphorus-rich globular bodies in young roots are probably Zn-phytate. Metallothioneins (MTs) are cysteine (Cys)-rich ligands. Plants produce class II MTs (MT-IIs) which differ from the archetypal mammalian MT-I in the location and number of Cys. The Ec protein from wheat embryos has Cys in three domains, binds Zn, and disappears with seedling development. The first 59 amino acids have been sequenced for the protein. Fifty-eight genes for MT-IIs, from a range of plants and tissues, predict proteins with Cys in two domains. Most of the predicted proteins have not been isolated, and their metal binding is poorly documented. Three protein bands, corresponding to six MT genes, have been isolated fromArabidopsis, and the amino acids sequenced for nine fragments. The MT-IIIs are atypical, nontranslationally synthesized polypeptides with variously repeating γ-glutamylcysteine units. Of the five families known, those with carboxy-terminal glycine are the most widespread among plants, algae, and certain yeasts. A heterogeneous grouping of these molecules form Cd-binding complexes with tetrahedral coordination and a Cd-sulfur interatomic distance of 2.52 Å. One complex is cytosolic, the dominant one is vacuolar. Together, they can bind a large proportion of cellular Cd; other ligands may also function. Little is known about the counterpart situation for Cu and Zn.