Structure and distinct supramolecular organization of a PSII-ACPII dimer from a cryptophyte alga Chroomonas placoidea

Zhiyuan Mao, Xingyue Li, Zhenhua Li, Liangliang Shen, Xiaoyi Li, Yanyan Yang, Wenda Wang, Tingyun Kuang, Jian-Ren Shen () and Guangye Han ()
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Zhiyuan Mao: Chinese Academy of Sciences
Xingyue Li: Chinese Academy of Sciences
Zhenhua Li: Chinese Academy of Sciences
Liangliang Shen: Chinese Academy of Sciences
Xiaoyi Li: Chinese Academy of Sciences
Yanyan Yang: Chinese Academy of Sciences
Wenda Wang: Chinese Academy of Sciences
Tingyun Kuang: Chinese Academy of Sciences
Jian-Ren Shen: Chinese Academy of Sciences
Guangye Han: Chinese Academy of Sciences

Nature Communications, 2024, vol. 15, issue 1, 1-14

Abstract: Abstract Cryptophyte algae are an evolutionarily distinct and ecologically important group of photosynthetic unicellular eukaryotes. Photosystem II (PSII) of cryptophyte algae associates with alloxanthin chlorophyll a/c-binding proteins (ACPs) to act as the peripheral light-harvesting system, whose supramolecular organization is unknown. Here, we purify the PSII-ACPII supercomplex from a cryptophyte alga Chroomonas placoidea (C. placoidea), and analyze its structure at a resolution of 2.47 Å using cryo-electron microscopy. This structure reveals a dimeric organization of PSII-ACPII containing two PSII core monomers flanked by six symmetrically arranged ACPII subunits. The PSII core is conserved whereas the organization of ACPII subunits exhibits a distinct pattern, different from those observed so far in PSII of other algae and higher plants. Furthermore, we find a Chl a-binding antenna subunit, CCPII-S, which mediates interaction of ACPII with the PSII core. These results provide a structural basis for the assembly of antennas within the supercomplex and possible excitation energy transfer pathways in cryptophyte algal PSII, shedding light on the diversity of supramolecular organization of photosynthetic machinery.

Date: 2024
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DOI: 10.1038/s41467-024-48878-x

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