2009 Fiscal Year Final Research Report
Elucidation of Cl--pumping mechanism and significance of trimer formation of halorhodopsin
| Project/Area Number |
19390009
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Physical pharmacy
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| Research Institution | Hokkaido University |
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Principal Investigator |
KAMO Naoki Hokkaido University, 薬学部, 教授 (10001976)
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| Co-Investigator(Kenkyū-buntansha) |
KIKUKAWA Takashi 北海道大学, 大学院・先端生命科学研究院, 教授 (20281842)
NARA Toshifumi 松山大学, 薬学部, 准教授 (30241350)
MIYAUCHI Seiji 松山大学, 薬学部, 教授 (30202352)
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| Project Period (FY) |
2007 – 2009
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| Keywords | ハロロドプシン / センソリーロドプシン / フォボロドプシン / レチナールタンパク / 高度好塩菌 / オーサイト / フォトサイクル / 閃光光分解 |
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| Research Abstract |
Halorhodopsin (HR) is a light-driven Cl^- pump expressed in the membrane of Halobacteria. We succeeded in developing a new method : HR was expressed in Xenopus laevis Oocytes, and photo-induced membrane current was measured due to the Cl^- transport. This method is highly quantitative. We prepared various HR mutants using E. coli expression system. Careful investigation on both the photochemistry and transport activities of the mutants has been done. We found Arg123 that is an essentially important amino acid residue. During the transition from N to O intermediate, Cl is released to cytoplasm while Cl is uptaken from extracellular space during O to HR' transition. We showed that HR forms trimer even in the presence of detergents, and that the trimer is more robust than the monomer.
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[Journal Article] Participation of the surface structure of pharaonis phoborhodopsin, ppR and its A149S and A149V mutants. Consisting of the C-terminal □-helix and E-F loop, in the complex-formation with the cognate transducer pHtrII, as revealed by site-directed 13C solidParticipati2007
Author(s)
I. Kawamura, Y. Ikeda, Y. Sudo, M. Iwamoto, K. Shimono, S. Yamaguchi, S. Tuzi, H. Saito, N. Kamo, A. Naito
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Journal Title
Photochem. Photobiol. 83
Pages: 339-345
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