TY - JOUR
T1 - Core and rod structures of a thermophilic cyanobacterial light-harvesting phycobilisome
AU - Kawakami, Keisuke
AU - Hamaguchi, Tasuku
AU - Hirose, Yuu
AU - Kosumi, Daisuke
AU - Miyata, Makoto
AU - Kamiya, Nobuo
AU - Yonekura, Koji
N1 - Funding Information:
We thank research assistants Ms. Yuko Kageyama (Biostructural Mechanism Laboratory, RIKEN SPring-8 Center) and Ms. Rie Uno (Osaka Metropolitan University) for their help with cell cultures, preparation of samples, electrophoresis analysis, and spectroscopy. We also thank Ms. Tomomi Shimonaka at the Graduate School of Science, Osaka City University, for performing MS/MS spectrometry. This work was supported by the Japan Society for the Promotion of Science (JSPS) (JP20H05109 (to KK), JP20K06528 (to K.K.), and JP17H06434 (to N.K.)) and partly by the Joint Usage/Research by Institute of Industrial Nanomaterials, Kumamoto University. JST-Mirai Program Grant Number JPMJMI20G5 (to K.Y.), and the Cyclic Innovation for Clinical Empowerment (CiCLE) from the Japan Agency for Medical Research and Development, AMED (to K.K., T.H., and K.Y.).
Publisher Copyright:
© 2022, The Author(s).
PY - 2022/12
Y1 - 2022/12
N2 - Cyanobacteria, glaucophytes, and rhodophytes utilize giant, light-harvesting phycobilisomes (PBSs) for capturing solar energy and conveying it to photosynthetic reaction centers. PBSs are compositionally and structurally diverse, and exceedingly complex, all of which pose a challenge for a comprehensive understanding of their function. To date, three detailed architectures of PBSs by cryo-electron microscopy (cryo-EM) have been described: a hemiellipsoidal type, a block-type from rhodophytes, and a cyanobacterial hemidiscoidal-type. Here, we report cryo-EM structures of a pentacylindrical allophycocyanin core and phycocyanin-containing rod of a thermophilic cyanobacterial hemidiscoidal PBS. The structures define the spatial arrangement of protein subunits and chromophores, crucial for deciphering the energy transfer mechanism. They reveal how the pentacylindrical core is formed, identify key interactions between linker proteins and the bilin chromophores, and indicate pathways for unidirectional energy transfer.
AB - Cyanobacteria, glaucophytes, and rhodophytes utilize giant, light-harvesting phycobilisomes (PBSs) for capturing solar energy and conveying it to photosynthetic reaction centers. PBSs are compositionally and structurally diverse, and exceedingly complex, all of which pose a challenge for a comprehensive understanding of their function. To date, three detailed architectures of PBSs by cryo-electron microscopy (cryo-EM) have been described: a hemiellipsoidal type, a block-type from rhodophytes, and a cyanobacterial hemidiscoidal-type. Here, we report cryo-EM structures of a pentacylindrical allophycocyanin core and phycocyanin-containing rod of a thermophilic cyanobacterial hemidiscoidal PBS. The structures define the spatial arrangement of protein subunits and chromophores, crucial for deciphering the energy transfer mechanism. They reveal how the pentacylindrical core is formed, identify key interactions between linker proteins and the bilin chromophores, and indicate pathways for unidirectional energy transfer.
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U2 - 10.1038/s41467-022-30962-9
DO - 10.1038/s41467-022-30962-9
M3 - Article
C2 - 35715389
AN - SCOPUS:85132117115
SN - 2041-1723
VL - 13
JO - Nature Communications
JF - Nature Communications
IS - 1
M1 - 3389
ER -