Light sensitive orange carotenoid proteins (OCPs) in cyanobacterial photoprotection: evolutionary insights, structural–functional dynamics and biotechnological prospects

IF 2.3 3区 生物学 Q3 MICROBIOLOGY Archives of Microbiology Pub Date : 2025-01-12 DOI:10.1007/s00203-024-04215-w
Syama Prabha, Aravind K. Vijay, Doniya Elze Mathew, Basil George
{"title":"Light sensitive orange carotenoid proteins (OCPs) in cyanobacterial photoprotection: evolutionary insights, structural–functional dynamics and biotechnological prospects","authors":"Syama Prabha,&nbsp;Aravind K. Vijay,&nbsp;Doniya Elze Mathew,&nbsp;Basil George","doi":"10.1007/s00203-024-04215-w","DOIUrl":null,"url":null,"abstract":"<div><p>Among all photosynthetic life forms, cyanobacteria exclusively possess a water-soluble, light-sensitive carotenoprotein complex known as orange carotenoid proteins (OCPs), crucial for their photoprotective mechanisms. These protein complexes exhibit both structural and functional modularity, with distinct C-terminal (CTD) and N-terminal domains (NTD) serving as light-responsive sensor and effector regions, respectively. The majority of cyanobacterial genomes contain genes for OCP homologs and related proteins, highlighting their essential role in survival of the organism over time. Cyanobacterial photoprotection primarily involves the translocation of carotenoid entity into the NTD, leading to remarkable conformational changes in both domains and formation of metastable OCP<sup>R</sup>. Subsequently, OCP<sup>R</sup> interacts with phycobiliprotein, inducing the quenching of excitation energy and a significant reduction in PS II fluorescence yield. In dark conditions, OCP<sup>R</sup> detaches from phycobilisomes and reverts to OCP<sup>O</sup> in the presence of fluorescent recovery proteins (FRP), sustaining a continuous cycle. Research suggests that the modular structure of the OCPs, coupled with its unique light-driven dissociation and re-association capability, opens avenues for exploiting its potential as light-controlled switches, offering various biotechnological applications.</p></div>","PeriodicalId":8279,"journal":{"name":"Archives of Microbiology","volume":"207 2","pages":""},"PeriodicalIF":2.3000,"publicationDate":"2025-01-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Archives of Microbiology","FirstCategoryId":"99","ListUrlMain":"https://link.springer.com/article/10.1007/s00203-024-04215-w","RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"MICROBIOLOGY","Score":null,"Total":0}
引用次数: 0

Abstract

Among all photosynthetic life forms, cyanobacteria exclusively possess a water-soluble, light-sensitive carotenoprotein complex known as orange carotenoid proteins (OCPs), crucial for their photoprotective mechanisms. These protein complexes exhibit both structural and functional modularity, with distinct C-terminal (CTD) and N-terminal domains (NTD) serving as light-responsive sensor and effector regions, respectively. The majority of cyanobacterial genomes contain genes for OCP homologs and related proteins, highlighting their essential role in survival of the organism over time. Cyanobacterial photoprotection primarily involves the translocation of carotenoid entity into the NTD, leading to remarkable conformational changes in both domains and formation of metastable OCPR. Subsequently, OCPR interacts with phycobiliprotein, inducing the quenching of excitation energy and a significant reduction in PS II fluorescence yield. In dark conditions, OCPR detaches from phycobilisomes and reverts to OCPO in the presence of fluorescent recovery proteins (FRP), sustaining a continuous cycle. Research suggests that the modular structure of the OCPs, coupled with its unique light-driven dissociation and re-association capability, opens avenues for exploiting its potential as light-controlled switches, offering various biotechnological applications.

查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
蓝藻光保护中的光敏橙色类胡萝卜素蛋白(OCPs):进化见解、结构-功能动力学和生物技术前景
在所有光合作用生命形式中,蓝藻只拥有一种水溶性、光敏的胡萝卜素蛋白复合物,即橙色类胡萝卜素蛋白(ocp),这对它们的光保护机制至关重要。这些蛋白复合物表现出结构和功能的模块化,具有不同的c端(CTD)和n端结构域(NTD),分别作为光响应传感器和效应区。大多数蓝藻基因组包含OCP同源基因和相关蛋白质,突出了它们在生物体生存中的重要作用。蓝藻的光保护主要涉及类胡萝卜素实体在NTD中的易位,导致两个结构域的显着构象变化和亚稳态OCPR的形成。随后,OCPR与藻胆蛋白相互作用,诱导激发能的猝灭和PS II荧光产率的显著降低。在黑暗条件下,OCPR从藻胆体上分离,并在荧光恢复蛋白(FRP)存在下还原为OCPO,维持一个连续的循环。研究表明,ocp的模块化结构,加上其独特的光驱动解离和再结合能力,为开发其作为光控开关的潜力开辟了道路,提供了各种生物技术应用。
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 去求助
来源期刊
Archives of Microbiology
Archives of Microbiology 生物-微生物学
CiteScore
4.90
自引率
3.60%
发文量
601
审稿时长
3 months
期刊介绍: Research papers must make a significant and original contribution to microbiology and be of interest to a broad readership. The results of any experimental approach that meets these objectives are welcome, particularly biochemical, molecular genetic, physiological, and/or physical investigations into microbial cells and their interactions with their environments, including their eukaryotic hosts. Mini-reviews in areas of special topical interest and papers on medical microbiology, ecology and systematics, including description of novel taxa, are also published. Theoretical papers and those that report on the analysis or ''mining'' of data are acceptable in principle if new information, interpretations, or hypotheses emerge.
期刊最新文献
Beyond the pink: uncovering the secrets of pink pigmented facultative methylotrophs Although invisible, fungi are recognized as the engines of a microbial powerhouse that drives soil ecosystem services Antibacterial and anti-biofilm activities of Derazantinib (ARQ-087) against Staphylococcus aureus Characterization of melanin from the fungus Scolecobasidium Musae and its antioxidant and photoprotective properties Akkermansia muciniphila: promises and pitfallsfor next-generation beneficial microorganisms
×
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
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术
文献互助 智能选刊 最新文献 互助须知 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 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1