LOV (light, oxygen, or voltage) domains of the blue-light photoreceptor phototropin (nph1): Binding sites for the chromophore flavin mononucleotide
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- John M. Christie
- Department of Plant Biology, Carnegie Institution of Washington, 260 Panama Street, Stanford, CA 94305; Botanisches Institut der Unversitaet Muenchen, Menzinger Strasse 67, D-80638 Muenchen, Germany; Department of Biology, Faculty of Science, Tokyo Metropolitan University, Minami-osawa 1-1, Hachioji-shi, 192-0397, Department of Plant Physiology, National Institute of Agrobiological Resources, 2-1-2 Kannondai, Tsukuba, Ibaraki 305, and Department of Regulation Biology, National Institute for Basic...
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- Michael Salomon
- Department of Plant Biology, Carnegie Institution of Washington, 260 Panama Street, Stanford, CA 94305; Botanisches Institut der Unversitaet Muenchen, Menzinger Strasse 67, D-80638 Muenchen, Germany; Department of Biology, Faculty of Science, Tokyo Metropolitan University, Minami-osawa 1-1, Hachioji-shi, 192-0397, Department of Plant Physiology, National Institute of Agrobiological Resources, 2-1-2 Kannondai, Tsukuba, Ibaraki 305, and Department of Regulation Biology, National Institute for Basic...
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- Kazunari Nozue
- Department of Plant Biology, Carnegie Institution of Washington, 260 Panama Street, Stanford, CA 94305; Botanisches Institut der Unversitaet Muenchen, Menzinger Strasse 67, D-80638 Muenchen, Germany; Department of Biology, Faculty of Science, Tokyo Metropolitan University, Minami-osawa 1-1, Hachioji-shi, 192-0397, Department of Plant Physiology, National Institute of Agrobiological Resources, 2-1-2 Kannondai, Tsukuba, Ibaraki 305, and Department of Regulation Biology, National Institute for Basic...
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- Masamitsu Wada
- Department of Plant Biology, Carnegie Institution of Washington, 260 Panama Street, Stanford, CA 94305; Botanisches Institut der Unversitaet Muenchen, Menzinger Strasse 67, D-80638 Muenchen, Germany; Department of Biology, Faculty of Science, Tokyo Metropolitan University, Minami-osawa 1-1, Hachioji-shi, 192-0397, Department of Plant Physiology, National Institute of Agrobiological Resources, 2-1-2 Kannondai, Tsukuba, Ibaraki 305, and Department of Regulation Biology, National Institute for Basic...
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- Winslow R. Briggs
- Department of Plant Biology, Carnegie Institution of Washington, 260 Panama Street, Stanford, CA 94305; Botanisches Institut der Unversitaet Muenchen, Menzinger Strasse 67, D-80638 Muenchen, Germany; Department of Biology, Faculty of Science, Tokyo Metropolitan University, Minami-osawa 1-1, Hachioji-shi, 192-0397, Department of Plant Physiology, National Institute of Agrobiological Resources, 2-1-2 Kannondai, Tsukuba, Ibaraki 305, and Department of Regulation Biology, National Institute for Basic...
書誌事項
- 公開日
- 1999-07-20
- DOI
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- 10.1073/pnas.96.15.8779
- 公開者
- Proceedings of the National Academy of Sciences
この論文をさがす
説明
<jats:p> Phototropism, the bending response of plant organs to or away from a directional light source, is one of the best studied blue light responses in plants. Although phototropism has been studied for more than a century, recent advances have improved our understanding of the underlying signaling mechanisms involved. The <jats:italic>NPH1</jats:italic> gene of <jats:italic>Arabidopsis thaliana</jats:italic> encodes a blue light-dependent autophosphorylating protein kinase with the properties of a photoreceptor for phototropism. NPH1 apoprotein noncovalently binds FMN to form the holoprotein nph1. The N-terminal region of the protein contains two LOV (light, oxygen, or voltage) domains that share homology with sensor proteins from a diverse group of organisms. These include the bacterial proteins NIFL and AER, both of which bind FAD, and the phy3 photoreceptor from <jats:italic>Adiantium capillus-veneris</jats:italic> . The LOV domain has therefore been proposed to reflect a flavin-binding site, regulating nph1 kinase activity in response to blue light-induced redox changes. Herein we demonstrate that the LOV domains of two nph1 proteins and phy3 bind stoichiometric amounts of FMN when expressed in <jats:italic>Escherichia coli.</jats:italic> The spectral properties of the chromopeptides are similar to the action spectrum for phototropism, implying that the LOV domain binds FMN to function as a light sensor. Thus, our findings support the earlier model that nph1 is a dual-chromophoric flavoprotein photoreceptor regulating phototropic responses in higher plants. We therefore propose the name phototropin to designate the nph1 holoprotein. </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 96 (15), 8779-8783, 1999-07-20
Proceedings of the National Academy of Sciences
