Response regulators implicated in His-to-Asp phosphotransfer signaling in <i>Arabidopsis</i>
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- Aya Imamura
- Laboratory of Molecular Microbiology, School of Agriculture, Nagoya University, Chikusa-ku, Nagoya 464, Japan
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- Naoto Hanaki
- Laboratory of Molecular Microbiology, School of Agriculture, Nagoya University, Chikusa-ku, Nagoya 464, Japan
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- Hiroyuki Umeda
- Laboratory of Molecular Microbiology, School of Agriculture, Nagoya University, Chikusa-ku, Nagoya 464, Japan
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- Ayako Nakamura
- Laboratory of Molecular Microbiology, School of Agriculture, Nagoya University, Chikusa-ku, Nagoya 464, Japan
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- Tomomi Suzuki
- Laboratory of Molecular Microbiology, School of Agriculture, Nagoya University, Chikusa-ku, Nagoya 464, Japan
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- Chiharu Ueguchi
- Laboratory of Molecular Microbiology, School of Agriculture, Nagoya University, Chikusa-ku, Nagoya 464, Japan
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- 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>
収録刊行物
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- Proceedings of the National Academy of Sciences
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Proceedings of the National Academy of Sciences 95 (5), 2691-2696, 1998-03-03
Proceedings of the National Academy of Sciences
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詳細情報 詳細情報について
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- CRID
- 1363951793233914880
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- NII論文ID
- 80010220800
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- ISSN
- 10916490
- 00278424
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