The Unique Light-Harvesting System of the Algal Phycobilisome: Structure, Assembly Components, and Functions
The phycobilisome (PBS) is the major light-harvesting apparatus in cyanobacteria and red algae. It is a large multi-subunit protein complex of several megadaltons that is found on the stromal side of thylakoid membranes in orderly arrays. Chromophore lyases catalyse the thioether bond between apopro...
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Published in | International journal of molecular sciences Vol. 24; no. 11; p. 9733 |
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Language | English |
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Abstract | The phycobilisome (PBS) is the major light-harvesting apparatus in cyanobacteria and red algae. It is a large multi-subunit protein complex of several megadaltons that is found on the stromal side of thylakoid membranes in orderly arrays. Chromophore lyases catalyse the thioether bond between apoproteins and phycobilins of PBSs. Depending on the species, composition, spatial assembly, and, especially, the functional tuning of different phycobiliproteins mediated by linker proteins, PBSs can absorb light between 450 and 650 nm, making them efficient and versatile light-harvesting systems. However, basic research and technological innovations are needed, not only to understand their role in photosynthesis but also to realise the potential applications of PBSs. Crucial components including phycobiliproteins, phycobilins, and lyases together make the PBS an efficient light-harvesting system, and these provide a scheme to explore the heterologous synthesis of PBS. Focusing on these topics, this review describes the essential components needed for PBS assembly, the functional basis of PBS photosynthesis, and the applications of phycobiliproteins. Moreover, key technical challenges for heterologous biosynthesis of phycobiliproteins in chassis cells are discussed. |
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AbstractList | The phycobilisome (PBS) is the major light-harvesting apparatus in cyanobacteria and red algae. It is a large multi-subunit protein complex of several megadaltons that is found on the stromal side of thylakoid membranes in orderly arrays. Chromophore lyases catalyse the thioether bond between apoproteins and phycobilins of PBSs. Depending on the species, composition, spatial assembly, and, especially, the functional tuning of different phycobiliproteins mediated by linker proteins, PBSs can absorb light between 450 and 650 nm, making them efficient and versatile light-harvesting systems. However, basic research and technological innovations are needed, not only to understand their role in photosynthesis but also to realise the potential applications of PBSs. Crucial components including phycobiliproteins, phycobilins, and lyases together make the PBS an efficient light-harvesting system, and these provide a scheme to explore the heterologous synthesis of PBS. Focusing on these topics, this review describes the essential components needed for PBS assembly, the functional basis of PBS photosynthesis, and the applications of phycobiliproteins. Moreover, key technical challenges for heterologous biosynthesis of phycobiliproteins in chassis cells are discussed. |
Audience | Academic |
Author | Li, Xiang Wang, Qiang Chen, Hui Lei, Jiaxi Hou, Wenwen |
AuthorAffiliation | 2 Academy for Advanced Interdisciplinary Studies, Henan University, Kaifeng 475001, China 1 State Key Laboratory of Crop Stress Adaptation and Improvement, School of Life Sciences, Henan University, Kaifeng 475004, China; lixiangx@mail.ustc.edu.cn (X.L.) |
AuthorAffiliation_xml | – name: 2 Academy for Advanced Interdisciplinary Studies, Henan University, Kaifeng 475001, China – name: 1 State Key Laboratory of Crop Stress Adaptation and Improvement, School of Life Sciences, Henan University, Kaifeng 475004, China; lixiangx@mail.ustc.edu.cn (X.L.) |
Author_xml | – sequence: 1 givenname: Xiang orcidid: 0000-0002-3558-2237 surname: Li fullname: Li, Xiang organization: State Key Laboratory of Crop Stress Adaptation and Improvement, School of Life Sciences, Henan University, Kaifeng 475004, China – sequence: 2 givenname: Wenwen surname: Hou fullname: Hou, Wenwen organization: State Key Laboratory of Crop Stress Adaptation and Improvement, School of Life Sciences, Henan University, Kaifeng 475004, China – sequence: 3 givenname: Jiaxi surname: Lei fullname: Lei, Jiaxi organization: State Key Laboratory of Crop Stress Adaptation and Improvement, School of Life Sciences, Henan University, Kaifeng 475004, China – sequence: 4 givenname: Hui surname: Chen fullname: Chen, Hui organization: State Key Laboratory of Crop Stress Adaptation and Improvement, School of Life Sciences, Henan University, Kaifeng 475004, China – sequence: 5 givenname: Qiang orcidid: 0000-0002-7388-4703 surname: Wang fullname: Wang, Qiang organization: Academy for Advanced Interdisciplinary Studies, Henan University, Kaifeng 475001, China |
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Keywords | assembly phycobilin photosynthesis phycobilisome biosynthesis phycobiliprotein |
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SubjectTerms | Algae Antioxidants assembly Biosynthesis Cancer Chlorophyll Chromophores Cosmetics Cyanobacteria Enzymes Heat resistance Photosynthesis phycobilin phycobiliprotein Phycobiliproteins phycobilisome Physiological aspects Proteins Review Solar energy Thylakoid membranes |
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Title | The Unique Light-Harvesting System of the Algal Phycobilisome: Structure, Assembly Components, and Functions |
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