TY - JOUR A1 - Leimkühler, Silke A1 - Lemaire, Olivier N. A1 - Iobbi-Nivol, Chantal T1 - Bacterial Molybdoenzymes BT - Chaperones, Assembly and Insertion JF - Molybdenum and tungsten enzymes : biochemistry N2 - The biogenesis of molybdoenzymes is a cytoplasmic event requiring both the folded apoenzymes and the matured molybdenum cofactor. The structure and the complexity of the molybdenum cofactor varies in each molybdoenzyme family and consequently different accessory proteins are required for the maturation of the respective enzymes. Thus, for enzymes of both the DMSO reductase and xanthine oxidase families, specific chaperones exist which are dedicated to increase the stability and the folding of specific members of each family. In this review, we describe the role of these chaperones for molybdoenzyme maturation. We present a model which describes step by step the mechanism of the maturation of representative molybdoenzymes from each family. Y1 - 2016 SN - 978-1-78262-391-5 SN - 978-1-78262-089-1 U6 - https://doi.org/10.1039/9781782623915-00117 VL - 5 SP - 117 EP - 142 PB - Royal Society of Chemistry CY - Cambridge ER - TY - JOUR A1 - Lemaire, Olivier N. A1 - Honore, Flora A. A1 - Tempel, Sebastien A1 - Fortier, Emma M. A1 - Leimkühler, Silke A1 - Mejean, Vincent A1 - Iobbi-Nivol, Chantal T1 - Shewanella decolorationis LDS1 Chromate Resistance JF - Applied and environmental microbiology N2 - The genus Shewanella is well known for its genetic diversity, its outstanding respiratory capacity, and its high potential for bioremediation. Here, a novel strain isolated from sediments of the Indian Ocean was characterized. A 16S rRNA analysis indicated that it belongs to the species Shewanella decolorationis. It was named Shewanella decolorationis LDS1. This strain presented an unusual ability to grow efficiently at temperatures from 24 degrees C to 40 degrees C without apparent modifications of its metabolism, as shown by testing respiratory activities or carbon assimilation, and in a wide range of salt concentrations. Moreover, S. decolorationis LDS1 tolerates high chromate concentrations. Indeed, it was able to grow in the presence of 4 mM chromate at 28 degrees C and 3 mM chromate at 40 degrees C. Interestingly, whatever the temperature, when the culture reached the stationary phase, the strain reduced the chromate present in the growth medium. In addition, S. decolorationis LDS1 degrades different toxic dyes, including anthraquinone, triarylmethane, and azo dyes. Thus, compared to Shewanella oneidensis, this strain presented better capacity to cope with various abiotic stresses, particularly at high temperatures. The analysis of genome sequence preliminary data indicated that, in contrast to S. oneidensis and S. decolorationis S12, S. decolorationis LDS1 possesses the phosphorothioate modification machinery that has been described as participating in survival against various abiotic stresses by protecting DNA. We demonstrate that its heterologous production in S. oneidensis allows it to resist higher concentrations of chromate. IMPORTANCE Shewanella species have long been described as interesting microorganisms in regard to their ability to reduce many organic and inorganic compounds, including metals. However, members of the Shewanella genus are often depicted as cold-water microorganisms, although their optimal growth temperature usually ranges from 25 to 28 degrees C under laboratory growth conditions. Shewanella decolorationis LDS1 is highly attractive, since its metabolism allows it to develop efficiently at temperatures from 24 to 40 degrees C, conserving its ability to respire alternative substrates and to reduce toxic compounds such as chromate or toxic dyes. Our results clearly indicate that this novel strain has the potential to be a powerful tool for bioremediation and unveil one of the mechanisms involved in its chromate resistance. KW - Shewanella KW - bioremediation KW - chromium KW - decolorization KW - dndBCDE KW - dyes KW - temperature Y1 - 2019 U6 - https://doi.org/10.1128/AEM.00777-19 SN - 0099-2240 SN - 1098-5336 VL - 85 IS - 18 PB - American Society for Microbiology CY - Washington ER - TY - GEN A1 - Lemaire, Olivier N. A1 - Infossi, Pascale A1 - Chaouche, Amine Ali A1 - Espinosa, Leon A1 - Leimkühler, Silke A1 - Giudici-Orticoni, Marie-Thérèse A1 - Méjean, Vincent A1 - Iobbi-Nivol, Chantal T1 - Small membranous proteins of the TorE/NapE family, crutches for cognate respiratory systems in Proteobacteria T2 - Postprints der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe N2 - In this report, we investigate small proteins involved in bacterial alternative respiratory systems that improve the enzymatic efficiency through better anchorage and multimerization of membrane components. Using the small protein TorE of the respiratory TMAO reductase system as a model, we discovered that TorE is part of a subfamily of small proteins that are present in proteobacteria in which they play a similar role for bacterial respiratory systems. We reveal by microscopy that, in Shewanella oneidensis MR1, alternative respiratory systems are evenly distributed in the membrane contrary to what has been described for Escherichia coli. Thus, the better efficiency of the respiratory systems observed in the presence of the small proteins is not due to a specific localization in the membrane, but rather to the formation of membranous complexes formed by TorE homologs with their c-type cytochrome partner protein. By an in vivo approach combining Clear Native electrophoresis and fluorescent translational fusions, we determined the 4: 4 stoichiometry of the complexes. In addition, mild solubilization of the cytochrome indicates that the presence of the small protein reinforces its anchoring to the membrane. Therefore, assembly of the complex induced by this small protein improves the efficiency of the respiratory system. T3 - Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe - 933 KW - trimethylamine n-oxide KW - molybdenum cofactor biosynthesis KW - cytochrome bd oxidase KW - c-type cytochromes KW - escherichia-coli KW - swiss-model KW - native electrophoresis KW - mutational analysis KW - reductase KW - nitrate KW - microbiology KW - microbiology techniques Y1 - 2020 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus4-459208 SN - 1866-8372 IS - 933 ER - TY - JOUR A1 - Lemaire, Olivier N. A1 - Infossi, Pascale A1 - Chaouche, Amine Ali A1 - Espinosa, Leon A1 - Leimkühler, Silke A1 - Giudici-Orticoni, Marie-Therese A1 - Mejean, Vincent A1 - Iobbi-Nivol, Chantal T1 - Small membranous proteins of the TorE/NapE family, crutches for cognate respiratory systems in Proteobacteria JF - Scientific reports N2 - In this report, we investigate small proteins involved in bacterial alternative respiratory systems that improve the enzymatic efficiency through better anchorage and multimerization of membrane components. Using the small protein TorE of the respiratory TMAO reductase system as a model, we discovered that TorE is part of a subfamily of small proteins that are present in proteobacteria in which they play a similar role for bacterial respiratory systems. We reveal by microscopy that, in Shewanella oneidensis MR1, alternative respiratory systems are evenly distributed in the membrane contrary to what has been described for Escherichia coli. Thus, the better efficiency of the respiratory systems observed in the presence of the small proteins is not due to a specific localization in the membrane, but rather to the formation of membranous complexes formed by TorE homologs with their c-type cytochrome partner protein. By an in vivo approach combining Clear Native electrophoresis and fluorescent translational fusions, we determined the 4: 4 stoichiometry of the complexes. In addition, mild solubilization of the cytochrome indicates that the presence of the small protein reinforces its anchoring to the membrane. Therefore, assembly of the complex induced by this small protein improves the efficiency of the respiratory system. Y1 - 2018 U6 - https://doi.org/10.1038/s41598-018-31851-2 SN - 2045-2322 VL - 8 PB - Nature Publ. Group CY - London ER -