{"title":"非常规嗜热型 C-phycocyanin 的分解和重组。","authors":"Hung Khac Nguyen , Takuo Minato , Takamasa Teramoto , Seiji Ogo , Yoshimitsu Kakuta , Ki-Seok Yoon","doi":"10.1016/j.jbiosc.2023.12.015","DOIUrl":null,"url":null,"abstract":"<div><p><span><span>C-phycocyanin (CPC), which contains open-chain tetrapyrroles, is a major light-harvesting red-fluorescent protein with an important role in aquatic </span>photosynthesis. Recently, we reported a non-conventional CPC from </span><em>Thermoleptolyngbya</em> sp. O-77 (CPC<sub>O77</sub>) that contains two different structures, i.e., a hexameric structure and a non-conventional octameric structure. However, the assembly and disassembly mechanisms of the non-conventional octameric form of CPC remain unclear. To understand this assembly mechanism, we performed an <em>in vitro</em> experiment to study the disassembly and reassembly behaviors of CPC using isolated CPC subunits. The dissociation of the CPC<sub>O77</sub><span><span> subunit was performed using a Phenyl-Sepharose column in 20 mM potassium phosphate buffer (pH 6.0) containing 7.0 M urea. For the first time, crystals of isolated CPC subunits were obtained and analyzed after separation. After the removal of urea from the purified α and </span>β subunits, we performed an </span><em>in vitro</em> reassembly experiment for CPC and analyzed the reconstructed CPC using spectrophotometric and X-ray crystal structure analyses. The crystal structure of the reassembled CPC was nearly identical to that of the original CPC<sub>O77</sub>. The findings of this study indicate that the octameric CPC<sub>O77</sub><span> is a naturally occurring form in the thermophilic cyanobacterium </span><em>Thermoleptolyngbya</em> sp. O-77.</p></div>","PeriodicalId":15199,"journal":{"name":"Journal of bioscience and bioengineering","volume":null,"pages":null},"PeriodicalIF":2.3000,"publicationDate":"2024-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Disassembly and reassembly of the non-conventional thermophilic C-phycocyanin\",\"authors\":\"Hung Khac Nguyen , Takuo Minato , Takamasa Teramoto , Seiji Ogo , Yoshimitsu Kakuta , Ki-Seok Yoon\",\"doi\":\"10.1016/j.jbiosc.2023.12.015\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p><span><span>C-phycocyanin (CPC), which contains open-chain tetrapyrroles, is a major light-harvesting red-fluorescent protein with an important role in aquatic </span>photosynthesis. Recently, we reported a non-conventional CPC from </span><em>Thermoleptolyngbya</em> sp. O-77 (CPC<sub>O77</sub>) that contains two different structures, i.e., a hexameric structure and a non-conventional octameric structure. However, the assembly and disassembly mechanisms of the non-conventional octameric form of CPC remain unclear. To understand this assembly mechanism, we performed an <em>in vitro</em> experiment to study the disassembly and reassembly behaviors of CPC using isolated CPC subunits. The dissociation of the CPC<sub>O77</sub><span><span> subunit was performed using a Phenyl-Sepharose column in 20 mM potassium phosphate buffer (pH 6.0) containing 7.0 M urea. For the first time, crystals of isolated CPC subunits were obtained and analyzed after separation. After the removal of urea from the purified α and </span>β subunits, we performed an </span><em>in vitro</em> reassembly experiment for CPC and analyzed the reconstructed CPC using spectrophotometric and X-ray crystal structure analyses. The crystal structure of the reassembled CPC was nearly identical to that of the original CPC<sub>O77</sub>. The findings of this study indicate that the octameric CPC<sub>O77</sub><span> is a naturally occurring form in the thermophilic cyanobacterium </span><em>Thermoleptolyngbya</em> sp. O-77.</p></div>\",\"PeriodicalId\":15199,\"journal\":{\"name\":\"Journal of bioscience and bioengineering\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":2.3000,\"publicationDate\":\"2024-03-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of bioscience and bioengineering\",\"FirstCategoryId\":\"5\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S1389172323003791\",\"RegionNum\":4,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q3\",\"JCRName\":\"BIOTECHNOLOGY & APPLIED MICROBIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of bioscience and bioengineering","FirstCategoryId":"5","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S1389172323003791","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"BIOTECHNOLOGY & APPLIED MICROBIOLOGY","Score":null,"Total":0}
Disassembly and reassembly of the non-conventional thermophilic C-phycocyanin
C-phycocyanin (CPC), which contains open-chain tetrapyrroles, is a major light-harvesting red-fluorescent protein with an important role in aquatic photosynthesis. Recently, we reported a non-conventional CPC from Thermoleptolyngbya sp. O-77 (CPCO77) that contains two different structures, i.e., a hexameric structure and a non-conventional octameric structure. However, the assembly and disassembly mechanisms of the non-conventional octameric form of CPC remain unclear. To understand this assembly mechanism, we performed an in vitro experiment to study the disassembly and reassembly behaviors of CPC using isolated CPC subunits. The dissociation of the CPCO77 subunit was performed using a Phenyl-Sepharose column in 20 mM potassium phosphate buffer (pH 6.0) containing 7.0 M urea. For the first time, crystals of isolated CPC subunits were obtained and analyzed after separation. After the removal of urea from the purified α and β subunits, we performed an in vitro reassembly experiment for CPC and analyzed the reconstructed CPC using spectrophotometric and X-ray crystal structure analyses. The crystal structure of the reassembled CPC was nearly identical to that of the original CPCO77. The findings of this study indicate that the octameric CPCO77 is a naturally occurring form in the thermophilic cyanobacterium Thermoleptolyngbya sp. O-77.
期刊介绍:
The Journal of Bioscience and Bioengineering is a research journal publishing original full-length research papers, reviews, and Letters to the Editor. The Journal is devoted to the advancement and dissemination of knowledge concerning fermentation technology, biochemical engineering, food technology and microbiology.