Structural basis for different types of hetero-tetrameric light-harvesting complexes in a diatom PSII-FCPII supercomplex

Ryo Nagao (), Koji Kato, Minoru Kumazawa, Kentaro Ifuku, Makio Yokono, Takehiro Suzuki, Naoshi Dohmae, Fusamichi Akita, Seiji Akimoto (), Naoyuki Miyazaki () and Jian-Ren Shen ()
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Ryo Nagao: Okayama University
Koji Kato: Okayama University
Minoru Kumazawa: Kyoto University
Kentaro Ifuku: Kyoto University
Makio Yokono: Hokkaido University
Takehiro Suzuki: Biomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science
Naoshi Dohmae: Biomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science
Fusamichi Akita: Okayama University
Seiji Akimoto: Kobe University
Naoyuki Miyazaki: University of Tsukuba
Jian-Ren Shen: Okayama University

Nature Communications, 2022, vol. 13, issue 1, 1-12

Abstract: Abstract Fucoxanthin chlorophyll (Chl) a/c-binding proteins (FCPs) function as light harvesters in diatoms. The structure of a diatom photosystem II-FCPII (PSII-FCPII) supercomplex have been solved by cryo-electron microscopy (cryo-EM) previously; however, the FCPII subunits that constitute the FCPII tetramers and monomers are not identified individually due to their low resolutions. Here, we report a 2.5 Å resolution structure of the PSII-FCPII supercomplex using cryo-EM. Two types of tetrameric FCPs, S-tetramer, and M-tetramer, are identified as different types of hetero-tetrameric complexes. In addition, three FCP monomers, m1, m2, and m3, are assigned to different gene products of FCP. The present structure also identifies the positions of most Chls c and diadinoxanthins, which form a complicated pigment network. Excitation-energy transfer from FCPII to PSII is revealed by time-resolved fluorescence spectroscopy. These structural and spectroscopic findings provide insights into an assembly model of FCPII and its excitation-energy transfer and quenching processes.

Date: 2022
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DOI: 10.1038/s41467-022-29294-5

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