Der Lysinexportcarrier in Corynebacterium glutamicum - Topologie und Regulation

Bellmann, A.

Dissertation / PhD Thesis/Book

Der Lysinexportcarrier in Corynebacterium glutamicum - Topologie und Regulation

Bellmann, A. (Corresponding author)FZJ*

2000
Forschungszentrum Jülich GmbH Zentralbibliothek, Verlag Jülich

Jülich : Forschungszentrum Jülich GmbH Zentralbibliothek, Verlag, Berichte des Forschungszentrums Jülich 3755, 97 S. (2000) = Düsseldorf, Univ., Diss., 2000

Please use a persistent id in citations: http://hdl.handle.net/2128/20603

Report No.: Juel-3755

Abstract: The L-Iysine export carrier LysE of the Gram-positive bacterium Corynebacterium gIptamisum represents the firnt funetionally analysed member of a new widespread superfamily of bacterial translocators . The results of phoA and IacZ fusion analysis of the topology of LysE suggest a unique topology for LysE . There is good evidence supporting a model in which LysE spans the cytoplasmic membrane five times with one additional hydrophobic domain which is most probably attached to the external side of the cytoplasmic membranei The putative regulator gene LysG is located adjacent to lysE and is divergently transcribed. Single-copy transcriptional fusions of lysE with lacZ show that LysG is a positive regulator of lysE expression enabling it to be induced up to 20-fold . This induction requires an inducer molecule . Using dipeptide feeding experiments intracellular L-Iysine, L-arginine, L-citrulline and L-histidine were shown to act as inducers an the LysG-mediated lysE expression . White L-arginine and L-Iysine are substrates of LysE this is not the oase for L-histidine and Lcitrulline . An in vivo experiment and gel shift studies provided evidence that LysG binds to the intergenic region of lysE and LysG. This region was delimited to 105 bp of this divergent promoter region of lysE and lysG .

Note: Record converted from VDB: 12.11.2012
Note: Düsseldorf, Univ., Diss., 2000

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