Funktion Eisen-transportierender CDF-Proteine in magnetotaktischen Bakterien und E. coli

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A specific subset of proteins that belong to the cation diffusion facilitator (CDF) family of membrane-bound transporters very frequently occurs in prokaryotes, but the physiological function of these proteins has remained obscure until recently. Data obtained for members of that family, Escherichia coli (FieF, former name Yiip) and Magnetospirillum gryphiswaldense (MamB, MamM), indicate that these proteins might transport Fe(II) and be part of the cellular iron homeostasis system in bacteria. E.coli and FieF are easy to manipulate by the methods of molecular genetics. MamB and MamM, on the orther hand are putative iron transporters with unusual properties since magnetosome biomineralization requires the transport of vast amounts of iron. In addition, M. gryphiswaldense has recently become amenable by genetic techniques, and magnetosome formation is a unique and conspicuous phenomenon. Therefore, the groups in Halle and Bremen joined forces to engage into the highly competitive field of iron transport by CDF proteins in an interlinked back-to-back approach: The physiological functions and biochemical mechanism of FieF and CDF-like Mam-proteins involved in magnetosome biosynthesis will be studied using a highly intergrated genetic, biochemical and physological approach. Ultimately, we not only expect to unveil the metabolic relevance of the specified proteins in iron homeostasis and magnetosome formation, respectively, but we will be able to assign a function to the whole family of so far uncharacterized CDF3 proteins.