TY - JOUR
T1 - Structural basis for assembly and function of a diatom photosystem I-light-harvesting supercomplex
AU - Nagao, Ryo
AU - Kato, Koji
AU - Ifuku, Kentaro
AU - Suzuki, Takehiro
AU - Kumazawa, Minoru
AU - Uchiyama, Ikuo
AU - Kashino, Yasuhiro
AU - Dohmae, Naoshi
AU - Akimoto, Seiji
AU - Shen, Jian Ren
AU - Miyazaki, Naoyuki
AU - Akita, Fusamichi
N1 - Funding Information:
This work was supported by the Platform Project for Supporting Drug Discovery and Life Science Research (Basis for Supporting Innovative Drug Discovery and Life Science Research (BINDS)) from AMED, PRESTO from JST grant No. JPMJPR16P1 (F.A.), JSPS KAKENHI grant Nos. JP17K07442, JP19H04726 (R.N.), JP16H06553 (S.A.), JP17H06433 (J.-R.S.), Advanced Low Carbon Technology Research, and Development Program from the Japan Science and Technology Agency grant No. JPMJAL1105 (Y.K. and K.I.), the joint usage/research program of the Artificial Photosynthesis Osaka City University (R.N.), and a Collaborative Research Program from National Institute for Basic Biology grant No. 19-455 (K.I.). We thank Ms. Hiroyo Nishide, NIBB, for supporting the genome data analysis.
Publisher Copyright:
© 2020, The Author(s).
PY - 2020/12/1
Y1 - 2020/12/1
N2 - Photosynthetic light-harvesting complexes (LHCs) play a pivotal role in collecting solar energy for photochemical reactions in photosynthesis. One of the major LHCs are fucoxanthin chlorophyll a/c-binding proteins (FCPs) present in diatoms, a group of organisms having important contribution to the global carbon cycle. Here, we report a 2.40-Å resolution structure of the diatom photosystem I (PSI)-FCPI supercomplex by cryo-electron microscopy. The supercomplex is composed of 16 different FCPI subunits surrounding a monomeric PSI core. Each FCPI subunit showed different protein structures with different pigment contents and binding sites, and they form a complicated pigment–protein network together with the PSI core to harvest and transfer the light energy efficiently. In addition, two unique, previously unidentified subunits were found in the PSI core. The structure provides numerous insights into not only the light-harvesting strategy in diatom PSI-FCPI but also evolutionary dynamics of light harvesters among oxyphototrophs.
AB - Photosynthetic light-harvesting complexes (LHCs) play a pivotal role in collecting solar energy for photochemical reactions in photosynthesis. One of the major LHCs are fucoxanthin chlorophyll a/c-binding proteins (FCPs) present in diatoms, a group of organisms having important contribution to the global carbon cycle. Here, we report a 2.40-Å resolution structure of the diatom photosystem I (PSI)-FCPI supercomplex by cryo-electron microscopy. The supercomplex is composed of 16 different FCPI subunits surrounding a monomeric PSI core. Each FCPI subunit showed different protein structures with different pigment contents and binding sites, and they form a complicated pigment–protein network together with the PSI core to harvest and transfer the light energy efficiently. In addition, two unique, previously unidentified subunits were found in the PSI core. The structure provides numerous insights into not only the light-harvesting strategy in diatom PSI-FCPI but also evolutionary dynamics of light harvesters among oxyphototrophs.
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U2 - 10.1038/s41467-020-16324-3
DO - 10.1038/s41467-020-16324-3
M3 - Article
C2 - 32424145
AN - SCOPUS:85084888130
SN - 2041-1723
VL - 11
JO - Nature communications
JF - Nature communications
IS - 1
M1 - 2481
ER -