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Nitrogen regulation of transport operons: analysis of promoters argTr and dhuA
Authors:Gudrun Schmitz  Peter Dürre  Guy Mullenbach and Giovanna Ferro-Luzzi Ames
Institution:(1) Department of Molecular Biology, Boehringer Manheim GmbH, Biochemical Research Center, Am Nonnenwald, D-8122 Penzberg, Federal Republic of Germany;(2) Institut für Mikrobiologie, Universität Göttingen, Grisebachstr. 8, D-3400 Göttingen, Federal Republic of Germany;(3) Chiron Research Laboratories, Chiron Corporation, 94608 Emeryville, CA, USA;(4) Department of Biochemistry, University of California, 94720 Berkeley, CA, USA
Abstract:Summary In Salmonella typhimurium the periplasmic permeases for histidine and for lysine-arginine-ornithine are regulated by nitrogen availability. The nature of the dhuA and argTr promoters of the operons coding for these permeases was analyzed by placing the galactokinase gene under their control (in vector pKO-1). argTr was found to respond to nitrogen regulation. We investigated the involvement of a mirror symmetry in argTr in its regulation by nitrogen. It had been postulated previously (Higgins and Ames 1982) that mirror symmetries might act as protein recognition sites important in regulation of gene expression. Here we demonstrate that the mirror symmetry in argTr is not involved in nitrogen control. Contrary to expectation, the galK gene was not regulated by nitrogen when it was placed under dhuA control. Here we propose a possible explanation for this finding.
Keywords:Nitrogen regulation  Mirror symmetry  Periplasmic permease  Promoters
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