Response regulators implicated in His-to-Asp phosphotransfer signaling in <i>Arabidopsis</i>

  • Aya Imamura
    Laboratory of Molecular Microbiology, School of Agriculture, Nagoya University, Chikusa-ku, Nagoya 464, Japan
  • Naoto Hanaki
    Laboratory of Molecular Microbiology, School of Agriculture, Nagoya University, Chikusa-ku, Nagoya 464, Japan
  • Hiroyuki Umeda
    Laboratory of Molecular Microbiology, School of Agriculture, Nagoya University, Chikusa-ku, Nagoya 464, Japan
  • Ayako Nakamura
    Laboratory of Molecular Microbiology, School of Agriculture, Nagoya University, Chikusa-ku, Nagoya 464, Japan
  • Tomomi Suzuki
    Laboratory of Molecular Microbiology, School of Agriculture, Nagoya University, Chikusa-ku, Nagoya 464, Japan
  • Chiharu Ueguchi
    Laboratory of Molecular Microbiology, School of Agriculture, Nagoya University, Chikusa-ku, Nagoya 464, Japan
  • Takeshi Mizuno
    Laboratory of Molecular Microbiology, School of Agriculture, Nagoya University, Chikusa-ku, Nagoya 464, Japan

抄録

<jats:p> The His to Asp phosphotransfer signal transduction mechanism involves three common signaling domains: the transmitter (or His-kinase), the receiver, and the histidine-containing phototransfer (HPt) domain. Typically, a sensor kinase has a His-kinase domain and a response regulator has a receiver domain containing a phosphoaccepting aspartate, whereas a histidine-containing phototransfer domain serves as a mediator of the histidine-to-aspartate phosphotransfer. This signal transduction mechanism was thought to be restricted to prokaryotes. However, many examples have been discovered in diverse eukaryotic species including higher plants. In <jats:italic>Arabidopsis</jats:italic> , three sensor kinases have been characterized, namely, ETR1, ERS, and CKI1, which were suggested to be involved in ethylene- and cytokinin-dependent signal transduction pathways, respectively. To date, no response regulator has been discovered in higher plants. We identify five distinct <jats:italic>Arabidopsis</jats:italic> response regulator genes, each encoding a protein containing a receiver-like domain. <jats:italic>In vivo</jats:italic> and <jats:italic>in vitro</jats:italic> evidence that ARRs can function as phosphoaccepting response regulators was obtained by employing the <jats:italic>Escherichia coli</jats:italic> His-Asp phosphotransfer signaling system. </jats:p>

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