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タイトル: | Single-molecule observation of the ligand-induced population shift of rhodopsin, a g-protein-coupled receptor. |
著者: | Maeda, Ryo Hiroshima, Michio Yamashita, Takahiro Wada, Akimori Nishimura, Shoko Sako, Yasushi Shichida, Yoshinori Imamoto, Yasushi https://orcid.org/0000-0002-0803-4163 (unconfirmed) |
著者名の別形: | 今元, 泰 |
発行日: | 18-Feb-2014 |
出版者: | Elsevier Inc. |
誌名: | Biophysical journal |
巻: | 106 |
号: | 4 |
開始ページ: | 915 |
終了ページ: | 924 |
抄録: | Rhodopsin is a G-protein-coupled receptor, in which retinal chromophore acts as inverse-agonist or agonist depending on its configuration and protonation state. Photostimulation of rhodopsin results in a pH-dependent equilibrium between the active state (Meta-II) and its inactive precursor (Meta-I). Here, we monitored conformational changes of rhodopsin using a fluorescent probe Alexa594 at the cytoplasmic surface, which shows fluorescence increase upon the generation of active state, by single-molecule measurements. The fluorescence intensity of a single photoactivated rhodopsin molecule alternated between two states. Interestingly, such a fluorescence alternation was also observed for ligand-free rhodopsin (opsin), but not for dark-state rhodopsin. In addition, the pH-dependences of Meta-I/Meta-II equilibrium estimated by fluorescence measurements deviated notably from estimates based on absorption spectra, indicating that both Meta-I and Meta-II are mixtures of two conformers. Our observations indicate that rhodopsin molecules intrinsically adopt both active and inactive conformations, and the ligand retinal shifts the conformational equilibrium. These findings provide dynamical insights into the activation mechanisms of G-protein-coupled receptors. |
著作権等: | © 2014 Biophysical Society. Published by Elsevier Inc. この論文は出版社版でありません。引用の際には出版社版をご確認ご利用ください。 This is not the published version. Please cite only the published version. |
URI: | http://hdl.handle.net/2433/185150 |
DOI(出版社版): | 10.1016/j.bpj.2014.01.020 |
PubMed ID: | 24559994 |
出現コレクション: | 学術雑誌掲載論文等 |
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