The tellurite-resistance determinants tehAtehB and klaAklaBtelB have different biochemical requirements

Article Abstract:

The ability of the Escherichia coli tehAtehB operon to confer resistance to potassium tellurite requires a specific metabolic state of the cell while the klaAklaBtelB operon functions independently of metabolic state. The tehAtehB operon requires a rich medium, the presence of an active electron transport system, a quinone pool and a cysteine metabolic pathway. The klaAklaBtelB operon does not require these host systems and is independent of the genotype. The two operons acts synergistically. The ter determinant in the IncHI2 operon also confers tellurite resistance.

Health aspects, Operons, Tellurium

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A novel and ubiquitous system for membrane targeting and secretion of cofactor-containing proteins

Article Abstract:

A study was conducted to identify the proteins encoded by the membrane targeting and translocation (mtt)ABC operon, which mediate a Sec-independent membrane targeting and translocation system in Escherichia coli that interacts with cofactor-containing redox proteins having a S/TRRXFLK twin arginine leader motif. Findings indicate that a mutation in mttA prevents the periplasmic localization of twin arginine redox enzymes. It also prevents the correct localization of the integral membrane molybeoenzyme dimethylsulfoxide reductase.

Membrane proteins

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Kinetic analysis and substrate specificity of Escherichia coli dimethyl sulfoxide reductase

Article Abstract:

The dimethyl sulfoxide reductase (DmsABC) iron-sulfur molybdoenzyme of Escherichia coli was analyzed to determine the parameters that affects substrate binding. The substrates of the complex DmsABC molybdoenzyme function as anaerobic terminal electron acceptors in wild-type cells. Furthermore, DmsAbC exhibited broad substrate specificity which is utilized for the synthesis of susbtituted pyridine N-oxides by Escherichia coli.

Microbial enzymes, Enzyme kinetics, Dimethyl sulfoxide

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