Involvement of the ribose operon repressor RbsR in regulation of purine nucleotide synthesis in Escherichia coli

Authors

  • Tomohiro Shimada,

    1. Department of Frontier Bioscience, Hosei University, Koganei, Tokyo, Japan
    2. Research Center for Micro-Nano Technology, Hosei University, Koganei, Tokyo, Japan
    3. Chemical Resources Laboratory, Tokyo Institute of Technology, Nagatsuda, Yokohama, Japan
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  • Ayako Kori,

    1. Department of Frontier Bioscience, Hosei University, Koganei, Tokyo, Japan
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  • Akira Ishihama

    Corresponding author
    1. Research Center for Micro-Nano Technology, Hosei University, Koganei, Tokyo, Japan
    • Department of Frontier Bioscience, Hosei University, Koganei, Tokyo, Japan
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Correspondence: Akira Ishihama, Hosei University, Department of Frontier Bioscience, Kajino-cho 3-7-2, Koganei, Tokyo 184-8584, Japan. Tel.: +81 42 3876231; fax: +81 42 3876231; e-mail: aishiham@hosei.ac.jp

Abstract

Escherichia coli is able to utilize d-ribose as its sole carbon source. The genes for the transport and initial-step metabolism of d-ribose form a single rbsDACBK operon. RbsABC forms the ABC-type high-affinity d-ribose transporter, while RbsD and RbsK are involved in the conversion of d-ribose into d-ribose 5-phosphate. In the absence of inducer d-ribose, the ribose operon is repressed by a LacI-type transcription factor RbsR, which is encoded by a gene located downstream of this ribose operon. At present, the rbs operon is believed to be the only target of regulation by RbsR. After Genomic SELEX screening, however, we have identified that RbsR binds not only to the rbs promoter but also to the promoters of a set of genes involved in purine nucleotide metabolism. Northern blotting analysis indicated that RbsR represses the purHD operon for de novo synthesis of purine nucleotide but activates the add and udk genes involved in the salvage pathway of purine nucleotide synthesis. Taken together, we propose that RbsR is a global regulator for switch control between the de novo synthesis of purine nucleotides and its salvage pathway.

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