Creation of photocyclic vertebrate rhodopsin by single amino acid substitution
Opsins are universal photoreceptive proteins in animals and can be classified into three types based on their photoreaction properties. Upon light irradiation, vertebrate rhodopsin forms a metastable active state, which cannot revert back to the original dark state via either photoreaction or therma...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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eLife Sciences Publications Ltd
2022-02-01
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| Series: | eLife |
| Subjects: | |
| Online Access: | https://elifesciences.org/articles/75979 |
| _version_ | 1811227359588646912 |
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| author | Kazumi Sakai Yoshinori Shichida Yasushi Imamoto Takahiro Yamashita |
| author_facet | Kazumi Sakai Yoshinori Shichida Yasushi Imamoto Takahiro Yamashita |
| author_sort | Kazumi Sakai |
| collection | DOAJ |
| description | Opsins are universal photoreceptive proteins in animals and can be classified into three types based on their photoreaction properties. Upon light irradiation, vertebrate rhodopsin forms a metastable active state, which cannot revert back to the original dark state via either photoreaction or thermal reaction. By contrast, after photoreception, most opsins form a stable active state which can photoconvert back to the dark state. Moreover, we recently found a novel type of opsins whose activity is regulated by photocycling. However, the molecular mechanism underlying this diversification of opsins remains unknown. In this study, we showed that vertebrate rhodopsin acquired the photocyclic and photoreversible properties upon introduction of a single mutation at position 188. This revealed that the residue at position 188 contributes to the diversification of photoreaction properties of opsins by its regulation of the recovery from the active state to the original dark state. |
| first_indexed | 2024-04-12T09:41:11Z |
| format | Article |
| id | doaj.art-9505bb4fa5f042dca57d20aa9f797042 |
| institution | Directory Open Access Journal |
| issn | 2050-084X |
| language | English |
| last_indexed | 2024-04-12T09:41:11Z |
| publishDate | 2022-02-01 |
| publisher | eLife Sciences Publications Ltd |
| record_format | Article |
| series | eLife |
| spelling | doaj.art-9505bb4fa5f042dca57d20aa9f7970422022-12-22T03:38:04ZengeLife Sciences Publications LtdeLife2050-084X2022-02-011110.7554/eLife.75979Creation of photocyclic vertebrate rhodopsin by single amino acid substitutionKazumi Sakai0https://orcid.org/0000-0001-6631-8546Yoshinori Shichida1Yasushi Imamoto2https://orcid.org/0000-0002-0803-4163Takahiro Yamashita3https://orcid.org/0000-0002-7956-9288Department of Biophysics, Graduate School of Science, Kyoto University, Kyoto, JapanDepartment of Biophysics, Graduate School of Science, Kyoto University, Kyoto, Japan; Research Organization for Science and technology, Ritsumeikan University, Kusatsu, JapanDepartment of Biophysics, Graduate School of Science, Kyoto University, Kyoto, JapanDepartment of Biophysics, Graduate School of Science, Kyoto University, Kyoto, JapanOpsins are universal photoreceptive proteins in animals and can be classified into three types based on their photoreaction properties. Upon light irradiation, vertebrate rhodopsin forms a metastable active state, which cannot revert back to the original dark state via either photoreaction or thermal reaction. By contrast, after photoreception, most opsins form a stable active state which can photoconvert back to the dark state. Moreover, we recently found a novel type of opsins whose activity is regulated by photocycling. However, the molecular mechanism underlying this diversification of opsins remains unknown. In this study, we showed that vertebrate rhodopsin acquired the photocyclic and photoreversible properties upon introduction of a single mutation at position 188. This revealed that the residue at position 188 contributes to the diversification of photoreaction properties of opsins by its regulation of the recovery from the active state to the original dark state.https://elifesciences.org/articles/75979rhodopsinretinalG protein-coupled receptor |
| spellingShingle | Kazumi Sakai Yoshinori Shichida Yasushi Imamoto Takahiro Yamashita Creation of photocyclic vertebrate rhodopsin by single amino acid substitution eLife rhodopsin retinal G protein-coupled receptor |
| title | Creation of photocyclic vertebrate rhodopsin by single amino acid substitution |
| title_full | Creation of photocyclic vertebrate rhodopsin by single amino acid substitution |
| title_fullStr | Creation of photocyclic vertebrate rhodopsin by single amino acid substitution |
| title_full_unstemmed | Creation of photocyclic vertebrate rhodopsin by single amino acid substitution |
| title_short | Creation of photocyclic vertebrate rhodopsin by single amino acid substitution |
| title_sort | creation of photocyclic vertebrate rhodopsin by single amino acid substitution |
| topic | rhodopsin retinal G protein-coupled receptor |
| url | https://elifesciences.org/articles/75979 |
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