Investigations on the structure, mechanism and evolution of the bacterial periplasmic transport system have been carried out on Z. mobilis and E. coli. During this work a glutamate/aspartate uptake system and the regulator grp (glutamate uptake regulary protein) have been isolated from Z. mobilis and subjected to a detailed characterization. Several regulary functions of the grp could be proved in E. coli. Gpr acts in a leucine-independent manner as an activator of the ilvIH operon, and it enhances the expression of a glutamate uptake system. At the same time it was demonstrated that grp reprimizes the expression of the glutamate/aspartate uptake system GluEMP isolated from Z. Moblis. Expression of grp in Z. mobilis and E. coli was studied by means of lacZ-mobilis and E. colie was studied by means of lacZ-gene fusion. In these experiments also a new regulatory function of the lrp was found: lrp enhances the expression of the binding protein-dependent glutamate uptake system of E. coli. (WEN)SIGLEAvailable from TIB Hannover: RA 831(3000) / FIZ - Fachinformationszzentrum Karlsruhe / TIB - Technische InformationsbibliothekDEGerman
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