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dc.contributor.authorSato, Keita-
dc.contributor.authorYamashita, Takahiro-
dc.contributor.authorOhuchi, Hideyo-
dc.contributor.authorTakeuchi, Atsuko-
dc.contributor.authorGotoh, Hitoshi-
dc.contributor.authorOno, Katsuhiko-
dc.contributor.authorMizuno, Misao-
dc.contributor.authorMizutani, Yasuhisa-
dc.contributor.authorTomonari, Sayuri-
dc.contributor.authorSakai, Kazumi-
dc.contributor.authorImamoto, Yasushi-
dc.contributor.authorWada, Akimori-
dc.contributor.authorShichida, Yoshinori-
dc.contributor.alternative佐藤, 恵太-
dc.contributor.alternative山下, 高廣-
dc.contributor.alternative大内, 淑代-
dc.contributor.alternative七田, 芳則-
dc.date.accessioned2018-04-04T23:57:02Z-
dc.date.available2018-04-04T23:57:02Z-
dc.date.issued2018-03-28-
dc.identifier.issn2041-1723-
dc.identifier.urihttp://hdl.handle.net/2433/230387-
dc.description光を受けるとオフになる動物のユニークな光センサーを発見 --ニワトリの脳内で機能するOpn5L1の性質を解明--. 京都大学プレスリリース. 2018-04-02.-
dc.description.abstractMost opsins are G protein-coupled receptors that utilize retinal both as a ligand and as a chromophore. Opsins’ main established mechanism is light-triggered activation through retinal 11-cis-to-all-trans photoisomerization. Here we report a vertebrate non-visual opsin that functions as a Gi-coupled retinal receptor that is deactivated by light and can thermally self-regenerate. This opsin, Opn5L1, binds exclusively to all-trans-retinal. More interestingly, the light-induced deactivation through retinal trans-to-cis isomerization is followed by formation of a covalent adduct between retinal and a nearby cysteine, which breaks the retinal-conjugated double bond system, probably at the C11 position, resulting in thermal re-isomerization to all-trans-retinal. Thus, Opn5L1 acts as a reverse photoreceptor. We conclude that, like vertebrate rhodopsin, Opn5L1 is a unidirectional optical switch optimized from an ancestral bidirectional optical switch, such as invertebrate rhodopsin, to increase the S/N ratio of the signal transduction, although the direction of optimization is opposite to that of vertebrate rhodopsin.-
dc.format.mimetypeapplication/pdf-
dc.language.isoeng-
dc.publisherSpringer Nature-
dc.rights© The Author(s) 2018. This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.-
dc.subjectBiochemistry-
dc.subjectG protein-coupled receptors-
dc.titleOpn5L1 is a retinal receptor that behaves as a reverse and self-regenerating photoreceptor-
dc.type.niitypeJournal Article-
dc.identifier.jtitleNature Communications-
dc.identifier.volume9-
dc.relation.doi10.1038/s41467-018-03603-3-
dc.textversionpublisher-
dc.identifier.artnum1255-
dc.identifier.pmid29593298-
dc.identifier.kaken25251036 / 16H02515 / 24115509 / 15H00812-
dc.relation.urlhttp://www.kyoto-u.ac.jp/ja/research/research_results/2017/170328_1.html-
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