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Uphill energy transfer mechanism for photosynthesis in an Antarctic alga

Author

Listed:
  • Makiko Kosugi

    (Astrobiology Center
    National Astronomical Observatory of Japan
    Chuo University
    National Institutes of Natural Science)

  • Masato Kawasaki

    (High Energy Accelerator Research Organization (KEK)
    The Graduate University of Advanced Studies (Soken-dai))

  • Yutaka Shibata

    (Tohoku University)

  • Kojiro Hara

    (Akita Prefectural University)

  • Shinichi Takaichi

    (Tokyo University of Agriculture)

  • Toshio Moriya

    (High Energy Accelerator Research Organization (KEK))

  • Naruhiko Adachi

    (High Energy Accelerator Research Organization (KEK))

  • Yasuhiro Kamei

    (National Institutes of Natural Sciences
    SOKENDAI (The Graduate University for Advanced Studies))

  • Yasuhiro Kashino

    (University of Hyogo)

  • Sakae Kudoh

    (National Institute of Polar Research, Research Organization of Information and Systems
    SOKENDAI (The Graduate University for Advanced Studies))

  • Hiroyuki Koike

    (Chuo University)

  • Toshiya Senda

    (High Energy Accelerator Research Organization (KEK)
    The Graduate University of Advanced Studies (Soken-dai)
    University of Tsukuba)

Abstract

Prasiola crispa, an aerial green alga, forms layered colonies under the severe terrestrial conditions of Antarctica. Since only far-red light is available at a deep layer of the colony, P. crispa has evolved a molecular system for photosystem II (PSII) excitation using far-red light with uphill energy transfer. However, the molecular basis underlying this system remains elusive. Here, we purified a light-harvesting chlorophyll (Chl)-binding protein complex from P. crispa (Pc-frLHC) that excites PSII with far-red light and revealed its ring-shaped structure with undecameric 11-fold symmetry at 3.13 Å resolution. The primary structure suggests that Pc-frLHC evolved from LHCI rather than LHCII. The circular arrangement of the Pc-frLHC subunits is unique among eukaryote LHCs and forms unprecedented Chl pentamers at every subunit‒subunit interface near the excitation energy exit sites. The Chl pentamers probably contribute to far-red light absorption. Pc-frLHC’s unique Chl arrangement likely promotes PSII excitation with entropy-driven uphill excitation energy transfer.

Suggested Citation

  • Makiko Kosugi & Masato Kawasaki & Yutaka Shibata & Kojiro Hara & Shinichi Takaichi & Toshio Moriya & Naruhiko Adachi & Yasuhiro Kamei & Yasuhiro Kashino & Sakae Kudoh & Hiroyuki Koike & Toshiya Senda, 2023. "Uphill energy transfer mechanism for photosynthesis in an Antarctic alga," Nature Communications, Nature, vol. 14(1), pages 1-14, December.
  • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-36245-1
    DOI: 10.1038/s41467-023-36245-1
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    References listed on IDEAS

    as
    1. Zhenfeng Liu & Hanchi Yan & Kebin Wang & Tingyun Kuang & Jiping Zhang & Lulu Gui & Xiaomin An & Wenrui Chang, 2004. "Crystal structure of spinach major light-harvesting complex at 2.72 Å resolution," Nature, Nature, vol. 428(6980), pages 287-292, March.
    2. Xuepeng Wei & Xiaodong Su & Peng Cao & Xiuying Liu & Wenrui Chang & Mei Li & Xinzheng Zhang & Zhenfeng Liu, 2016. "Structure of spinach photosystem II–LHCII supercomplex at 3.2 Å resolution," Nature, Nature, vol. 534(7605), pages 69-74, June.
    3. Adam Ben-Shem & Felix Frolow & Nathan Nelson, 2003. "Crystal structure of plant photosystem I," Nature, Nature, vol. 426(6967), pages 630-635, December.
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