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| Main Authors: | , , , , , , , , , , , , , , |
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| Format: | Artículo científico |
| Language: | en |
| Published: |
The Journal of biological chemistry
2025
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| Subjects: | |
| Online Access: | https://pubmed.ncbi.nlm.nih.gov/40436317/ |
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| _version_ | 1868266198712451074 |
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| author | Nagata, Yuya Miyamoto, Norio Sato, Keita Nishimura, Yosuke Tanioka, Yuki Yamanaka, Yuji Yoshizawa, Susumu Takahashi, Kuto Obayashi, Kohei Tsukamoto, Hisao Takai, Ken Ohuchi, Hideyo Yamashita, Takahiro Sudo, Yuki Kojima, Keiichi |
| author_facet | Nagata, Yuya Miyamoto, Norio Sato, Keita Nishimura, Yosuke Tanioka, Yuki Yamanaka, Yuji Yoshizawa, Susumu Takahashi, Kuto Obayashi, Kohei Tsukamoto, Hisao Takai, Ken Ohuchi, Hideyo Yamashita, Takahiro Sudo, Yuki Kojima, Keiichi Nagata, Yuya Miyamoto, Norio Sato, Keita Nishimura, Yosuke Tanioka, Yuki Yamanaka, Yuji Yoshizawa, Susumu Takahashi, Kuto Obayashi, Kohei Tsukamoto, Hisao Takai, Ken Ohuchi, Hideyo Yamashita, Takahiro Sudo, Yuki Kojima, Keiichi |
| collection | PubMed - marine biology |
| contents | A repertoire of visible light-sensitive opsins in the deep-sea hydrothermal vent shrimp Rimicaris hybisae. Nagata, Yuya Miyamoto, Norio Sato, Keita Nishimura, Yosuke Tanioka, Yuki Yamanaka, Yuji Yoshizawa, Susumu Takahashi, Kuto Obayashi, Kohei Tsukamoto, Hisao Takai, Ken Ohuchi, Hideyo Yamashita, Takahiro Sudo, Yuki Kojima, Keiichi Animals Light Hydrothermal Vents Opsins Decapoda Arthropod Proteins Phylogeny Crustacea Unlike terrestrial environments, where humans reside, there is no sunlight in the deep sea. Instead, dim visible light from black-body radiation and bioluminescence illuminates hydrothermal vent areas in the deep sea. A deep-sea hydrothermal vent shrimp, Rimicaris hybisae, is thought to detect this dim light using its enlarged dorsal eye; however, the molecular basis of its photoreception remains unexplored. Here, we characterized the molecular properties of opsins, universal photoreceptive proteins in animals, found in R. hybisae. Transcriptomic analysis identified six opsins: three Gq-coupled opsins, one Opn3, one Opn5, and one peropsin. Functional analysis revealed that five of these opsins exhibited light-dependent G protein activity, whereas peropsin exhibited the ability to convert all-trans-retinal to 11-cis-retinal like photoisomerases. Notably, all the R. hybisae opsins, including Opn5, convergently show visible light sensitivity (around 457-517 nm), whereas most opsins categorized as Opn5 have been demonstrated to be UV sensitive. Mutational analysis revealed that the unique visible light sensitivity of R. hybisae Opn5 is achieved through the stabilization of a protonated Schiff base by a counterion residue at position 83 (Asp83), which differs from the position identified in other opsins. These findings suggest that the vent shrimp R. hybisae has adapted its photoreceptive devices to dim deep-sea hydrothermal light by selectively maintaining a repertoire of visible light-sensitive opsins, including the uniquely tuned Opn5. |
| format | Artículo científico |
| id | pubmed_40436317 |
| institution | PubMed |
| language | en |
| publishDate | 2025 |
| publisher | The Journal of biological chemistry |
| record_format | pubmed |
| spellingShingle | A repertoire of visible light-sensitive opsins in the deep-sea hydrothermal vent shrimp Rimicaris hybisae. Nagata, Yuya Miyamoto, Norio Sato, Keita Nishimura, Yosuke Tanioka, Yuki Yamanaka, Yuji Yoshizawa, Susumu Takahashi, Kuto Obayashi, Kohei Tsukamoto, Hisao Takai, Ken Ohuchi, Hideyo Yamashita, Takahiro Sudo, Yuki Kojima, Keiichi Animals Light Hydrothermal Vents Opsins Decapoda Arthropod Proteins Phylogeny Crustacea A repertoire of visible light-sensitive opsins in the deep-sea hydrothermal vent shrimp Rimicaris hybisae. Nagata, Yuya Miyamoto, Norio Sato, Keita Nishimura, Yosuke Tanioka, Yuki Yamanaka, Yuji Yoshizawa, Susumu Takahashi, Kuto Obayashi, Kohei Tsukamoto, Hisao Takai, Ken Ohuchi, Hideyo Yamashita, Takahiro Sudo, Yuki Kojima, Keiichi Animals Light Hydrothermal Vents Opsins Decapoda Arthropod Proteins Phylogeny Crustacea Unlike terrestrial environments, where humans reside, there is no sunlight in the deep sea. Instead, dim visible light from black-body radiation and bioluminescence illuminates hydrothermal vent areas in the deep sea. A deep-sea hydrothermal vent shrimp, Rimicaris hybisae, is thought to detect this dim light using its enlarged dorsal eye; however, the molecular basis of its photoreception remains unexplored. Here, we characterized the molecular properties of opsins, universal photoreceptive proteins in animals, found in R. hybisae. Transcriptomic analysis identified six opsins: three Gq-coupled opsins, one Opn3, one Opn5, and one peropsin. Functional analysis revealed that five of these opsins exhibited light-dependent G protein activity, whereas peropsin exhibited the ability to convert all-trans-retinal to 11-cis-retinal like photoisomerases. Notably, all the R. hybisae opsins, including Opn5, convergently show visible light sensitivity (around 457-517 nm), whereas most opsins categorized as Opn5 have been demonstrated to be UV sensitive. Mutational analysis revealed that the unique visible light sensitivity of R. hybisae Opn5 is achieved through the stabilization of a protonated Schiff base by a counterion residue at position 83 (Asp83), which differs from the position identified in other opsins. These findings suggest that the vent shrimp R. hybisae has adapted its photoreceptive devices to dim deep-sea hydrothermal light by selectively maintaining a repertoire of visible light-sensitive opsins, including the uniquely tuned Opn5. |
| title | A repertoire of visible light-sensitive opsins in the deep-sea hydrothermal vent shrimp Rimicaris hybisae. |
| topic | Animals Light Hydrothermal Vents Opsins Decapoda Arthropod Proteins Phylogeny Crustacea |
| url | https://pubmed.ncbi.nlm.nih.gov/40436317/ |