ID 112465
Author
Sato, Keita Okayama University
Yamashita, Takahiro Kyoto University
Ohuchi, Hideyo Okayama University
Takeuchi, Atsuko Kobe Pharmaceutical University
Gotoh, Hitoshi Kyoto Prefectural University of Medicine
Ono, Katsuhiko Kyoto Prefectural University of Medicine
Mizuno, Misao Osaka University
Mizutani, Yasuhisa Osaka University
Tomonari, Sayuri Tokushima University
Sakai, Kazumi Kyoto University
Imamoto, Yasushi Kyoto University
Wada, Akimori Kobe Pharmaceutical University
Shichida, Yoshinori Kyoto University|Ritsumeikan University
Content Type
Journal Article
Description
Most 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.
Journal Title
Nature Communications
ISSN
20411723
NCID
AA12645905
Publisher
Springer Nature
Volume
9
Start Page
1255
Published Date
2018-03-28
Remark
Supplementary Information : ncomms_9_1255_s1.pdf
Peer Review File : ncomms_9_1255_s2.pdf
Rights
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/.
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DOI (Published Version)
URL ( Publisher's Version )
FullText File
language
eng
TextVersion
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departments
Technical Support Department