4.8 Article

Core and rod structures of a thermophilic cyanobacterial light-harvesting phycobilisome

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NATURE COMMUNICATIONS
卷 13, 期 1, 页码 -

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NATURE PORTFOLIO
DOI: 10.1038/s41467-022-30962-9

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  1. Japan Society for the Promotion of Science (JSPS) [JP20H05109, JP20K06528, JP17H06434]
  2. Institute of Industrial Nanomaterials, Kumamoto University
  3. JST-Mirai Program [JPMJMI20G5]

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In this study, the structures of a pentacylindrical core and rod in a thermophilic cyanobacterial phycobilisome were examined by cryo-electron microscopy. This research provides valuable insights into the energy transfer mechanism through the observation of protein subunit arrangement and chromophores.
Phycobilisome (PBS) absorbs solar energy and transfer the energy to photosynthetic membrane proteins. In this study, the structures of the pentacylindrical core and rod in PBS from a thermophilic cyanobacterium by cryo-electron microscopy. 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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