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Structure of a monomeric photosystem I core associated with iron-stress-induced-A proteins from Anabaena sp. PCC 7120

Author

Listed:
  • Ryo Nagao

    (Okayama University
    Shizuoka University)

  • Koji Kato

    (Okayama University
    Japan Synchrotron Radiation Research Institute (JASRI))

  • Tasuku Hamaguchi

    (RIKEN SPring-8 Center
    Tohoku University)

  • Yoshifumi Ueno

    (Kobe University
    Tokyo University of Science)

  • Naoki Tsuboshita

    (Okayama University)

  • Shota Shimizu

    (Okayama University)

  • Miyu Furutani

    (Kobe University)

  • Shigeki Ehira

    (Tokyo Metropolitan University)

  • Yoshiki Nakajima

    (Okayama University)

  • Keisuke Kawakami

    (RIKEN SPring-8 Center)

  • Takehiro Suzuki

    (Biomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science)

  • Naoshi Dohmae

    (Biomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science)

  • Seiji Akimoto

    (Kobe University)

  • Koji Yonekura

    (RIKEN SPring-8 Center
    Tohoku University
    Advanced Electron Microscope Development Unit, RIKEN-JEOL Collaboration Center, RIKEN Baton Zone Program)

  • Jian-Ren Shen

    (Okayama University)

Abstract

Iron-stress-induced-A proteins (IsiAs) are expressed in cyanobacteria under iron-deficient conditions. The cyanobacterium Anabaena sp. PCC 7120 has four isiA genes; however, their binding property and functional roles in PSI are still missing. We analyzed a cryo-electron microscopy structure of a PSI-IsiA supercomplex isolated from Anabaena grown under an iron-deficient condition. The PSI-IsiA structure contains six IsiA subunits associated with the PsaA side of a PSI core monomer. Three of the six IsiA subunits were identified as IsiA1 and IsiA2. The PSI-IsiA structure lacks a PsaL subunit; instead, a C-terminal domain of IsiA2 occupies the position of PsaL, which inhibits the oligomerization of PSI, leading to the formation of a PSI monomer. Furthermore, excitation-energy transfer from IsiAs to PSI appeared with a time constant of 55 ps. These findings provide insights into both the molecular assembly of the Anabaena IsiA family and the functional roles of IsiAs.

Suggested Citation

  • Ryo Nagao & Koji Kato & Tasuku Hamaguchi & Yoshifumi Ueno & Naoki Tsuboshita & Shota Shimizu & Miyu Furutani & Shigeki Ehira & Yoshiki Nakajima & Keisuke Kawakami & Takehiro Suzuki & Naoshi Dohmae & S, 2023. "Structure of a monomeric photosystem I core associated with iron-stress-induced-A proteins from Anabaena sp. PCC 7120," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-36504-1
    DOI: 10.1038/s41467-023-36504-1
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    References listed on IDEAS

    as
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