ホウライシダ フィトクロム3のLOV2ドメインの光活性化過程におけるGlu1029の役割 Role of Gln1029 in the Photoactivation Processes of the LOV2 Domain in <i>Adiantum</i> Phytochrome3

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Abstract

Phototropin (phot) is a blue-light receptor in plants. Phot has two FMN binding domains named LOV domain. In response to light absorption, a covalent adduct forms between a cysteine and FMN C(4a), which is called S390. According to the crystal structures of the LOV2 domain of <i>Adiantum</i> phytochrome3 (phy3), a chimeric phytochrome/phototropin, in the dark and S390 states, the side chain of Gln1029 switches hydrogen bond with FMN. <br>The structural changes were measured in the Q1029L mutant by low-temperature FTIR spectroscopy. It was implied that hydrogen-bond of FMN C(4)=O group is not formed in Q1029L. Upon formation of S390, hydrogen bond of C(4)=O becomes weaker in both WT and Q1029L. On the other hand, the protein structural changes of Q1029L were smaller than those of WT at room temperature.<br>These results suggest that the hydrogen-bonding interaction of Gln1029 with FMN plays an important role in the protein structural changes of phy3-LOV2.

Journal

  • Plant and Cell Physiology Supplement

    Plant and Cell Physiology Supplement 2004(0), 237-237, 2004

    The Japanese Society of Plant Physiologists

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