of the molecular mechanisms for Mg2+ transport in plants is very limited, with only three publications reporting a molecular basis for Mg2+ transport in plants. However, the importance of Mg2+ to plants has been well described, and physiological and ecophysiological studies about the effects of Mg2+ are numerous. This section will summarise the knowledge of a gene family identified in plants that is distantly related to CorA. Another gene, a Mg2+/H+ exchanger (AtMHX), unrelated to this gene family and to CorA has also been identified, is localised to the vacuolar membrane, and will be described last. The AtMRS2 gene family Schock et al. (2000) identified and named the family AtMRS2 based on the similarity of the genes to the MRS2 gene of yeast. The authors also showed that the AtMRS2-1 gene could complement a Δmrs2 yeast mutant phenotype. Independently, Li et al. (2001) published a report identifying the family and showing that two additional members could complement Mg2+ transport deficient mutants, one in S. typhimurium and the other in S. cerevisiae. The three genes that have been shown to transport Mg2+ are AtMRS2-1, AtMRS2-10 and AtMRS2-11, and these genes produce proteins 442, 443 and 459 amino acids in size, respectively. Each of the proteins shows significant similarity to Mrs2p of yeast and a weak similarity to CorA of bacteria, contains the conserved GMN amino acid motif at the outside end of the first TM domain, and is predicted to have two TM domains. The AtMRS2-1 gene, when expressed in yeast from the MRS2 promoter and being fused C-terminally to the first 95 amino acids of the Mrs2p protein, was directed to the mitochondria, where it complemented a Δmrs2 mutant both phenotypically (mitochondrial RNA splicing was restored) and with respect to the Mg2+ content of the organelle. No data on the kinetics of the transport was presented. The AtMRS2-11 gene was analysed in yeast (in the alr1 alr2 strain), where it was shown that expression of the gene significantly increased the rate of Mg2+ uptake into starved cells over the control, as measured using flame atomic absorption spectroscopy of total cellular Mg2+ content. However, Alr1p was shown to be significantly more effective at transporting Mg2+ at low extracellular concentrations, suggesting that the affinity of AtMRS2-11 for Mg2+ is lower than that of Alr1p. An electrophysiological (voltage clamp) analysis of the AtMRS2-11 protein in Xenopus oocytes also showed a Mg2+-dependent current at