A blue-shifted anion channelrhodopsin from the Colpodellida alga Vitrella brassicaformis
Abstract Microbial rhodopsins, a family of photoreceptive membrane proteins containing the chromophore retinal, show a variety of light-dependent molecular functions. Channelrhodopsins work as light-gated ion channels and are widely utilized for optogenetics, which is a method for controlling neural...
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| Format: | Article |
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Nature Portfolio
2023-04-01
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| Series: | Scientific Reports |
| Online Access: | https://doi.org/10.1038/s41598-023-34125-8 |
| _version_ | 1797836587756683264 |
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| author | Keiichi Kojima Shiho Kawanishi Yosuke Nishimura Masumi Hasegawa Shin Nakao Yuya Nagata Susumu Yoshizawa Yuki Sudo |
| author_facet | Keiichi Kojima Shiho Kawanishi Yosuke Nishimura Masumi Hasegawa Shin Nakao Yuya Nagata Susumu Yoshizawa Yuki Sudo |
| author_sort | Keiichi Kojima |
| collection | DOAJ |
| description | Abstract Microbial rhodopsins, a family of photoreceptive membrane proteins containing the chromophore retinal, show a variety of light-dependent molecular functions. Channelrhodopsins work as light-gated ion channels and are widely utilized for optogenetics, which is a method for controlling neural activities by light. Since two cation channelrhodopsins were identified from the chlorophyte alga Chlamydomonas reinhardtii, recent advances in genomic research have revealed a wide variety of channelrhodopsins including anion channelrhodopsins (ACRs), describing their highly diversified molecular properties (e.g., spectral sensitivity, kinetics and ion selectivity). Here, we report two channelrhodopsin-like rhodopsins from the Colpodellida alga Vitrella brassicaformis, which are phylogenetically distinct from the known channelrhodopsins. Spectroscopic and electrophysiological analyses indicated that these rhodopsins are green- and blue-sensitive pigments (λmax = ~ 550 and ~ 440 nm) that exhibit light-dependent ion channeling activities. Detailed electrophysiological analysis revealed that one of them works as a monovalent anion (Cl−, Br− and NO3 −) channel and we named it V. brassicaformis anion channelrhodopsin-2, VbACR2. Importantly, the absorption maximum of VbACR2 (~ 440 nm) is blue-shifted among the known ACRs. Thus, we identified the new blue-shifted ACR, which leads to the expansion of the molecular diversity of ACRs. |
| first_indexed | 2024-04-09T15:11:19Z |
| format | Article |
| id | doaj.art-f9aed3575bf544b7a8e4419ce581ea6a |
| institution | Directory Open Access Journal |
| issn | 2045-2322 |
| language | English |
| last_indexed | 2024-04-09T15:11:19Z |
| publishDate | 2023-04-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Scientific Reports |
| spelling | doaj.art-f9aed3575bf544b7a8e4419ce581ea6a2023-04-30T11:12:27ZengNature PortfolioScientific Reports2045-23222023-04-0113111110.1038/s41598-023-34125-8A blue-shifted anion channelrhodopsin from the Colpodellida alga Vitrella brassicaformisKeiichi Kojima0Shiho Kawanishi1Yosuke Nishimura2Masumi Hasegawa3Shin Nakao4Yuya Nagata5Susumu Yoshizawa6Yuki Sudo7Faculty of Medicine, Dentistry and Pharmaceutical Sciences, Okayama UniversityGraduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama UniversityResearch Center for Bioscience and Nanoscience (CeBN), Research Institute for Marine Resources Utilization, Japan Agency for Marine-Earth Science and Technology (JAMSTEC)Institute for Extra-Cutting-Edge Science and Technology Avant-Garde Research (X-Star), Japan Agency for Marine-Earth Science and Technology (JAMSTEC)Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama UniversityGraduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama UniversityAtmosphere and Ocean Research Institute, The University of TokyoFaculty of Medicine, Dentistry and Pharmaceutical Sciences, Okayama UniversityAbstract Microbial rhodopsins, a family of photoreceptive membrane proteins containing the chromophore retinal, show a variety of light-dependent molecular functions. Channelrhodopsins work as light-gated ion channels and are widely utilized for optogenetics, which is a method for controlling neural activities by light. Since two cation channelrhodopsins were identified from the chlorophyte alga Chlamydomonas reinhardtii, recent advances in genomic research have revealed a wide variety of channelrhodopsins including anion channelrhodopsins (ACRs), describing their highly diversified molecular properties (e.g., spectral sensitivity, kinetics and ion selectivity). Here, we report two channelrhodopsin-like rhodopsins from the Colpodellida alga Vitrella brassicaformis, which are phylogenetically distinct from the known channelrhodopsins. Spectroscopic and electrophysiological analyses indicated that these rhodopsins are green- and blue-sensitive pigments (λmax = ~ 550 and ~ 440 nm) that exhibit light-dependent ion channeling activities. Detailed electrophysiological analysis revealed that one of them works as a monovalent anion (Cl−, Br− and NO3 −) channel and we named it V. brassicaformis anion channelrhodopsin-2, VbACR2. Importantly, the absorption maximum of VbACR2 (~ 440 nm) is blue-shifted among the known ACRs. Thus, we identified the new blue-shifted ACR, which leads to the expansion of the molecular diversity of ACRs.https://doi.org/10.1038/s41598-023-34125-8 |
| spellingShingle | Keiichi Kojima Shiho Kawanishi Yosuke Nishimura Masumi Hasegawa Shin Nakao Yuya Nagata Susumu Yoshizawa Yuki Sudo A blue-shifted anion channelrhodopsin from the Colpodellida alga Vitrella brassicaformis Scientific Reports |
| title | A blue-shifted anion channelrhodopsin from the Colpodellida alga Vitrella brassicaformis |
| title_full | A blue-shifted anion channelrhodopsin from the Colpodellida alga Vitrella brassicaformis |
| title_fullStr | A blue-shifted anion channelrhodopsin from the Colpodellida alga Vitrella brassicaformis |
| title_full_unstemmed | A blue-shifted anion channelrhodopsin from the Colpodellida alga Vitrella brassicaformis |
| title_short | A blue-shifted anion channelrhodopsin from the Colpodellida alga Vitrella brassicaformis |
| title_sort | blue shifted anion channelrhodopsin from the colpodellida alga vitrella brassicaformis |
| url | https://doi.org/10.1038/s41598-023-34125-8 |
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