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Asymmetric structure of the native Rhodobacter sphaeroides dimeric LH1–RC complex

Author

Listed:
  • Kazutoshi Tani

    (Mie University)

  • Ryo Kanno

    (Okinawa Institute of Science and Technology Graduate University (OIST), 1919-1, Tancha, Onna-son, Kunigami-gun)

  • Riku Kikuchi

    (Ibaraki University)

  • Saki Kawamura

    (Ibaraki University)

  • Kenji V. P. Nagashima

    (Kanagawa University, 2946 Tsuchiya)

  • Malgorzata Hall

    (Okinawa Institute of Science and Technology Graduate University (OIST), 1919-1, Tancha, Onna-son, Kunigami-gun)

  • Ai Takahashi

    (Okinawa Institute of Science and Technology Graduate University (OIST), 1919-1, Tancha, Onna-son, Kunigami-gun)

  • Long-Jiang Yu

    (Photosynthesis Research Center, Key Laboratory of Photobiology, Institute of Botany, Chinese Academy of Sciences)

  • Yukihiro Kimura

    (Kobe University)

  • Michael T. Madigan

    (Southern Illinois University)

  • Akira Mizoguchi

    (Mie University)

  • Bruno M. Humbel

    (Okinawa Institute of Science and Technology Graduate University (OIST), 1919-1, Tancha, Onna-son, Kunigami-gun)

  • Zheng-Yu Wang-Otomo

    (Ibaraki University)

Abstract

Rhodobacter sphaeroides is a model organism in bacterial photosynthesis, and its light-harvesting-reaction center (LH1–RC) complex contains both dimeric and monomeric forms. Here we present cryo-EM structures of the native LH1–RC dimer and an LH1–RC monomer lacking protein-U (ΔU). The native dimer reveals several asymmetric features including the arrangement of its two monomeric components, the structural integrity of protein-U, the overall organization of LH1, and rigidities of the proteins and pigments. PufX plays a critical role in connecting the two monomers in a dimer, with one PufX interacting at its N-terminus with another PufX and an LH1 β-polypeptide in the other monomer. One protein-U was only partially resolved in the dimeric structure, signaling different degrees of disorder in the two monomers. The ΔU LH1–RC monomer was half-moon-shaped and contained 11 α- and 10 β-polypeptides, indicating a critical role for protein-U in controlling the number of αβ-subunits required for dimer assembly and stabilization. These features are discussed in relation to membrane topology and an assembly model proposed for the native dimeric complex.

Suggested Citation

  • Kazutoshi Tani & Ryo Kanno & Riku Kikuchi & Saki Kawamura & Kenji V. P. Nagashima & Malgorzata Hall & Ai Takahashi & Long-Jiang Yu & Yukihiro Kimura & Michael T. Madigan & Akira Mizoguchi & Bruno M. H, 2022. "Asymmetric structure of the native Rhodobacter sphaeroides dimeric LH1–RC complex," Nature Communications, Nature, vol. 13(1), pages 1-9, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-29453-8
    DOI: 10.1038/s41467-022-29453-8
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    References listed on IDEAS

    as
    1. Kazutoshi Tani & Kenji V. P. Nagashima & Ryo Kanno & Saki Kawamura & Riku Kikuchi & Malgorzata Hall & Long-Jiang Yu & Yukihiro Kimura & Michael T. Madigan & Akira Mizoguchi & Bruno M. Humbel & Zheng-Y, 2021. "A previously unrecognized membrane protein in the Rhodobacter sphaeroides LH1-RC photocomplex," Nature Communications, Nature, vol. 12(1), pages 1-9, December.
    2. Svetlana Bahatyrova & Raoul N. Frese & C. Alistair Siebert & John D. Olsen & Kees O. van der Werf & Rienk van Grondelle & Robert A. Niederman & Per A. Bullough & Cees Otto & C. Neil Hunter, 2004. "The native architecture of a photosynthetic membrane," Nature, Nature, vol. 430(7003), pages 1058-1062, August.
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