Role of Trp 104 in AppA BLUF domain as revealed by FTIR spectroscopy
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- Hasegawa Koji
- Molecular Membrane Laboratory, RIKEN
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- Masuda Shinji
- Graduate School of Bioscience and Biotechnology, Tokyo Institute of echnology
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- Ono Takaaki
- Molecular Membrane Laboratory, RIKEN
Bibliographic Information
- Other Title
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- 青色光受容体蛋白質AppAのTrp104の役割
Abstract
AppA is a member of a sensor of blue light using FAD (BLUF) protein family. In this study, effects of W104A mutation on spectroscopic properties of the AppA BLUF domain (AppA126) were investigated. The W104A mutant showed a nearly normal redshift in the UV-visible absorption of FAD upon illumination. However, the light state as revealed by the upshifted absorption relaxed to the dark state at a rate 150 times faster in the mutant than in the wild-type AppA126. The mutation led to 2cm-1 upshift of the C4=O stretch bands in the light-induced Fourier transform infrared (FTIR) spectrum. Notably, prominent protein bands assigned to the light-induced change of the β-sheet structure were markedly affected by the mutation to be eliminated and/or modified. These results indicate that Trp104 is responsible for transforming the light signal into a specific β-sheet structure change for the signaling state in the apoprotein of AppA BLUF domain.
Journal
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- Plant and Cell Physiology Supplement
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Plant and Cell Physiology Supplement 2006 (0), 536-536, 2006
The Japanese Society of Plant Physiologists
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Details 詳細情報について
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- CRID
- 1390001205626988032
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- NII Article ID
- 130006987090
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- Data Source
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- JaLC
- CiNii Articles
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- Abstract License Flag
- Disallowed