Isolation and Molecular Characterization of the Locked-on Mutant of Mg2+ Sensor PhoQ in Escherichia coli

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  • MINAGAWA Shu
    Department of Bioscience and Biotechnology, Graduate School of Agriculture, Kinki University
  • OKURA Ryouta
    Department of Bioscience and Biotechnology, Graduate School of Agriculture, Kinki University
  • TSUCHITANI Hiroki
    Department of Bioscience and Biotechnology, Graduate School of Agriculture, Kinki University
  • HIRAO Kiyo
    Department of Bioscience and Biotechnology, Graduate School of Agriculture, Kinki University
  • YAMAMOTO Kaneyoshi
    Department of Bioscience and Biotechnology, Graduate School of Agriculture, Kinki University
  • UTSUMI Ryutaro
    Department of Bioscience and Biotechnology, Graduate School of Agriculture, Kinki University

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  • Isolation and Molecular Characterization of the Locked-on Mutant of Mg〔2+〕 Sensor PhoQ in Escherichia coli
  • Isolation and Molecular Characterization of the Locked-on Mutant of Mg<sup>2+</sup>Sensor PhoQ in<i>Escherichia coli</i>

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A Mg2+ sensor mutant (PhoQD179L(A)) in which D179 of PhoQ was changed into L or A was isolated and characterized in Escherichia coli. PhoQ–PhoP regulon genes, phoPQ, mgtA and mgrB transcriptions were repressed at a high Mg2+ concentration in WQ3007 (phoQ-defective strain)/pHO119, but not in WQ3007/pHO179L(A). The in vitro autophosphorylation activity of membrane-bound PhoQ was repressed by Mg2+ (10 mM), but that of membrane-bound PhoQD179L(A) was not. Furthermore, the phosphotransfer from membrane-bound PhoQ to PhoP was also repressed by Mg2+, but was not observed in membrane-bound PhoQD179L(A). These results suggest that PhoQD179L(A) is a locked-on mutant that is defective in extracellular Mg2+-sensing and that the D179 amino acid residue of PhoQ plays an essential role in signal transfer between the Mg2+-sensory and histidine kinase domain of PhoQ.

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