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

• Nozaki Dai

  Department of Applied chemistry, Nagoya Institute of Technology

• Iwata Tatsuya

  Department of Applied chemistry, Nagoya Institute of Technology RIAST, University of Osaka Prefecture

• Ishikawa Tomoko

  Radiation Biology Center, Kyoto University

• Todo Takeshi

  Radiation Biology Center, Kyoto University

• Tokutomi Satoru

  RIAST, University of Osaka Prefecture

• Kandori Hideki

  Department of Applied chemistry, Nagoya Institute of Technology

書誌事項

タイトル別名

• Role of Gln1029 in the Photoactivation Processes of the LOV2 Domain in <i>Adiantum</i> Phytochrome3

抄録

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 Adiantum 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.

収録刊行物

• 日本植物生理学会年会およびシンポジウム　講演要旨集

  日本植物生理学会年会およびシンポジウム　講演要旨集 2004 (0), 237-237, 2004

  日本植物生理学会

詳細情報

• CRID: 1390282680603529984
• NII論文ID: 130006986938
• DOI: 10.14841/jspp.2004.0.237.0
• データソース種別:
  • JaLC
  • CiNii Articles
• 抄録ライセンスフラグ: 使用不可