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Structure of phycobilisome from the red alga Griffithsia pacifica

Author

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  • Jun Zhang

    (State Key Laboratory of Membrane Biology, Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University
    MRC Laboratory of Molecular Biology)

  • Jianfei Ma

    (State Key Laboratory of Membrane Biology, Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University)

  • Desheng Liu

    (State Key Laboratory of Membrane Biology, Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University)

  • Song Qin

    (Yantai Institute of Coast Zone Research, Chinese Academy of Sciences)

  • Shan Sun

    (State Key Laboratory of Membrane Biology, Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University)

  • Jindong Zhao

    (State Key Laboratory of Protein and Plant Genetic Engineering, College of Life Sciences, Peking University
    Key Laboratory of Phycology of CAS, Institute of Hydrobiology, Chinese Academy of Sciences)

  • Sen-Fang Sui

    (State Key Laboratory of Membrane Biology, Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University)

Abstract

Life on Earth depends on photosynthesis for its conversion of solar energy to chemical energy. Photosynthetic organisms have developed a variety of light-harvesting systems to capture sunlight. The largest light-harvesting complex is the phycobilisome (PBS), the main light-harvesting antenna in cyanobacteria and red algae. It is composed of phycobiliproteins and linker proteins but the assembly mechanisms and energy transfer pathways of the PBS are not well understood. Here we report the structure of a 16.8-megadalton PBS from a red alga at 3.5 Å resolution obtained by single-particle cryo-electron microscopy. We modelled 862 protein subunits, including 4 linkers in the core, 16 rod–core linkers and 52 rod linkers, and located a total of 2,048 chromophores. This structure reveals the mechanisms underlying specific interactions between linkers and phycobiliproteins, and the formation of linker skeletons. These results provide a firm structural basis for our understanding of complex assembly and the mechanisms of energy transfer within the PBS.

Suggested Citation

  • Jun Zhang & Jianfei Ma & Desheng Liu & Song Qin & Shan Sun & Jindong Zhao & Sen-Fang Sui, 2017. "Structure of phycobilisome from the red alga Griffithsia pacifica," Nature, Nature, vol. 551(7678), pages 57-63, November.
    • Handle: RePEc:nat:nature:v:551:y:2017:i:7678:d:10.1038_nature24278
    DOI: 10.1038/nature24278
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    Citations

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    Cited by:

    1. Alejandra Guillén-García & Savannah E. R. Gibson & Caleb J. C. Jordan & Venkata K. Ramaswamy & Victoria L. Linthwaite & Elizabeth H. C. Bromley & Adrian P. Brown & David R. W. Hodgson & Tim R. Blower , 2022. "Allophycocyanin A is a carbon dioxide receptor in the cyanobacterial phycobilisome," Nature Communications, Nature, vol. 13(1), pages 1-10, December.
    2. Zhiyuan Mao & Xingyue Li & Zhenhua Li & Liangliang Shen & Xiaoyi Li & Yanyan Yang & Wenda Wang & Tingyun Kuang & Jian-Ren Shen & Guangye Han, 2024. "Structure and distinct supramolecular organization of a PSII-ACPII dimer from a cryptophyte alga Chroomonas placoidea," Nature Communications, Nature, vol. 15(1), pages 1-14, December.
    3. Lvqin Zheng & Zhengdong Zhang & Hongrui Wang & Zhenggao Zheng & Jiayu Wang & Heyuan Liu & Hailong Chen & Chunxia Dong & Guopeng Wang & Yuxiang Weng & Ning Gao & Jindong Zhao, 2023. "Cryo-EM and femtosecond spectroscopic studies provide mechanistic insight into the energy transfer in CpcL-phycobilisomes," Nature Communications, Nature, vol. 14(1), pages 1-10, December.
    4. Han-Wei Jiang & Hsiang-Yi Wu & Chun-Hsiung Wang & Cheng-Han Yang & Jui-Tse Ko & Han-Chen Ho & Ming-Daw Tsai & Donald A. Bryant & Fay-Wei Li & Meng-Chiao Ho & Ming-Yang Ho, 2023. "A structure of the relict phycobilisome from a thylakoid-free cyanobacterium," Nature Communications, Nature, vol. 14(1), pages 1-14, December.
    5. Keisuke Kawakami & Tasuku Hamaguchi & Yuu Hirose & Daisuke Kosumi & Makoto Miyata & Nobuo Kamiya & Koji Yonekura, 2022. "Core and rod structures of a thermophilic cyanobacterial light-harvesting phycobilisome," Nature Communications, Nature, vol. 13(1), pages 1-13, December.
    6. Shivam Yadav & Martin Centola & Mathilda Glaesmann & Denys Pogoryelov & Roman Ladig & Mike Heilemann & L. C. Rai & Özkan Yildiz & Enrico Schleiff, 2022. "Cyclophilin anaCyp40 regulates photosystem assembly and phycobilisome association in a cyanobacterium," Nature Communications, Nature, vol. 13(1), pages 1-17, December.

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