Cnidopsins Characterized as Bistable Opsins From a Reef-Building Coral, Acropora tenuis.

IF 1 4区 生物学 Q3 ZOOLOGY
Yukiya Kakeyama, Yusuke Sakai, Tomohiro Sugihara, Mitsumasa Koyanagi, Akihisa Terakita
{"title":"Cnidopsins Characterized as Bistable Opsins From a Reef-Building Coral, <i>Acropora tenuis</i>.","authors":"Yukiya Kakeyama, Yusuke Sakai, Tomohiro Sugihara, Mitsumasa Koyanagi, Akihisa Terakita","doi":"10.2108/zs250032","DOIUrl":null,"url":null,"abstract":"<p><p>Many cnidarian animals possess multiple opsins, including a type known as cnidopsin, which is found throughout the phylum Cnidaria and is divided into several subgroups. Previous studies have suggested that cnidopsins from jellyfish and coral can light-dependently elevate intracellular cAMP levels, likely via activation of Gs-type G protein in cultured cells. However, their spectroscopic properties remain largely unclear, with the exception of jellyfish opsins. We recently identified eight cnidopsins from the reef-building coral <i>Acropora tenuis</i> and showed that they phylogenetically belong to different cnidopsin subgroups. Here, we spectroscopically analyzed one <i>A. tenuis</i> cnidopsin from each subgroup as a representative. We successfully obtained the absorption spectrum of one purified cnidopsin and found that it was blue-sensitive, with an absorption maximum at ∼460 nm. Blue light irradiation (460 nm) resulted in a red-shifted absorption spectrum, while subsequent irradiation with orange light (> 560 nm) caused a blue-shift. The difference spectra of after versus before repeated irradiation with alternating blue and orange light produced mirror images, indicating a bistable nature. We also successfully observed the absorption spectra of one of two other cnidopsins belonging to the same subgroup as the blue-sensitive <i>A. tenuis</i> cnidopsin. The spectral changes suggested that it was also a bistable opsin. These results suggest that these two coral cnidopsins, which belong to the same cnidopsin subgroup, are bistable-unlike jellyfish opsins, which belong to a different cnidopsin subgroup.</p>","PeriodicalId":24040,"journal":{"name":"Zoological Science","volume":"42 4","pages":""},"PeriodicalIF":1.0000,"publicationDate":"2025-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Zoological Science","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.2108/zs250032","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"ZOOLOGY","Score":null,"Total":0}
引用次数: 0

Abstract

Many cnidarian animals possess multiple opsins, including a type known as cnidopsin, which is found throughout the phylum Cnidaria and is divided into several subgroups. Previous studies have suggested that cnidopsins from jellyfish and coral can light-dependently elevate intracellular cAMP levels, likely via activation of Gs-type G protein in cultured cells. However, their spectroscopic properties remain largely unclear, with the exception of jellyfish opsins. We recently identified eight cnidopsins from the reef-building coral Acropora tenuis and showed that they phylogenetically belong to different cnidopsin subgroups. Here, we spectroscopically analyzed one A. tenuis cnidopsin from each subgroup as a representative. We successfully obtained the absorption spectrum of one purified cnidopsin and found that it was blue-sensitive, with an absorption maximum at ∼460 nm. Blue light irradiation (460 nm) resulted in a red-shifted absorption spectrum, while subsequent irradiation with orange light (> 560 nm) caused a blue-shift. The difference spectra of after versus before repeated irradiation with alternating blue and orange light produced mirror images, indicating a bistable nature. We also successfully observed the absorption spectra of one of two other cnidopsins belonging to the same subgroup as the blue-sensitive A. tenuis cnidopsin. The spectral changes suggested that it was also a bistable opsin. These results suggest that these two coral cnidopsins, which belong to the same cnidopsin subgroup, are bistable-unlike jellyfish opsins, which belong to a different cnidopsin subgroup.

造礁珊瑚Acropora tenuis中具有双稳态视蛋白特征的刺胞视蛋白。
许多刺胞动物拥有多种视蛋白,包括一种被称为刺胞蛋白的类型,它在刺胞动物门中被发现,并被分为几个亚群。先前的研究表明,水母和珊瑚中的刺胞嘧啶可以光依赖性地提高细胞内cAMP水平,可能是通过激活培养细胞中的gs型G蛋白来实现的。然而,除了水母视蛋白外,它们的光谱特性在很大程度上仍然不清楚。我们最近从造礁珊瑚Acropora tenuis中鉴定出8种刺胞蛋白,并表明它们在系统发育上属于不同的刺胞蛋白亚群。在这里,我们从每个亚群中选取了一种具有代表性的棘刺槐进行了光谱分析。我们成功地获得了一种纯化的刺胞嘧啶的吸收光谱,发现它对蓝敏感,在~ 460 nm处具有最大吸收。蓝光照射(460 nm)导致吸收光谱红移,而随后的橙光照射(> 560 nm)导致吸收光谱蓝移。蓝光和橙光交替照射前后的光谱差异产生镜像,表明双稳性。我们还成功地观察了另外两种与蓝敏感的刺胞嘧啶属于同一亚群的刺胞嘧啶中的一种的吸收光谱。光谱变化表明它也是一种双稳态视蛋白。这些结果表明,这两种珊瑚视蛋白是双稳态的,它们属于同一个视蛋白亚群,而水母视蛋白属于不同的视蛋白亚群。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 求助全文
来源期刊
Zoological Science
Zoological Science 生物-动物学
CiteScore
1.70
自引率
11.10%
发文量
59
审稿时长
1 months
期刊介绍: Zoological Science is published by the Zoological Society of Japan and devoted to publication of original articles, reviews and editorials that cover the broad field of zoology. The journal was founded in 1984 as a result of the consolidation of Zoological Magazine (1888–1983) and Annotationes Zoologicae Japonenses (1897–1983), the former official journals of the Zoological Society of Japan. Each annual volume consists of six regular issues, one every two months.
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:604180095
Book学术官方微信