Becker A, Bergès H, Krol E, Bruand C, Rüberg S, Capela D, Lauber

Becker A, Bergès H, Krol E, Bruand C, Rüberg S, Capela D, Lauber E, Meilhoc E, Ampe F, De Bruijn FJ, et al.: Global changes in gene 4SC-202 chemical structure expression in Sinorhizobium meliloti 1021 under microoxic and symbiotic conditions. Mol Plant Microbe Interact 2004,17(3):292–303.PubMedCrossRef 46. Pandey SP, Minesinger BK, Kumar J, Walker GC: A highly conserved protein of unknown function in Sinorhizobium meliloti affects sRNA regulation similar to Hfq. Nucleic Acids Res 2011,39(11):4691–4708.PubMedCentralPubMedCrossRef

47. Miller JH: Molecular genetics experiments. Cold Spring Harbor, N.Y: Cold Spring Harbor Laboratory; 1972. Competing interests The authors declared they have no competing interests. Authors’ contributions CMD, VP and AMG collected and analysed data. AMG and JB directed the work. JB and CMB wrote and revised the manuscript. All authors have read and approved the final version of this manuscript.”
“Background A number of Gram-negative bacteria can grow anaerobically through dissimilatory reduction of metals such as insoluble Fe(III) and Mn(IV) oxides [1]. Among these, the genus of Shewanella has been

a focus of research for its versatile capabilities of dissimilatory metal reduction, which has potentials for bioremediation of toxic metals [2–4]. Because of its metabolic capabilities, Shewanella is widely distributed in diverse habitats of soil, fresh water, marine water and even hydrothermal vents, with a preference of residing in stratified environments [2, 5, 6]. The most studied strain of Shewanella is undoubtedly S. oneidensis MR-1. It has been well established that some genes of an mtrBAC-omcA-mtrFED gene cluster of MR-1, such selleck compound as mtrBAC and omcA, is involved in Fe(III), Mn(IV) and U (VI) reduction. This cluster contains two genes (mtrC and omcA) encoding outer membrane Quisinostat c-type cytochromes that form a protein complex [7] and function as a terminal reductase towards solid-phase metal (hydr)oxides. To facilitate the interaction with the solid-phase metal(hydr)oxides, these two cytochromes

are organized in that MtrC is spatially distributed on Depsipeptide chemical structure cell surface while OmcA is localized between cell surface and minerals, as shown by antibody-recognition force microscopy [8]. Consistently, the presence of both MtrC and OmcA was required for reduction of solid-phase metal(hydr)oxides [9–11]. In comparison, not much is known about the specific functions of mtrFED. Recently, it was reported that ΔmtrD showed no deficiency in reducing soluble and insoluble Fe(III), but soluble Fe(III) reduction of the mutant was progressively slower when mtrA was also absent, implicating a role in Fe(III) reduction [12]. Similarly, ΔmtrF alone showed no deficiency in reducing soluble and insoluble Fe(III), but ΔmtrF/ΔmtrC was incapable of insoluble Fe(III) reduction. The recent availability of whole genome sequences in dozens of Shewanella species has made it possible to examine the gene cluster of metal reduction in other members of the genus.

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