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Cryo-EM structures of thylakoid-located voltage-dependent chloride channel VCCN1

Author

Listed:
  • Tatsuya Hagino

    (The University of Tokyo)

  • Takafumi Kato

    (The University of Tokyo
    University of Oxford)

  • Go Kasuya

    (Jichi Medical University)

  • Kan Kobayashi

    (The University of Tokyo
    Peptidream Inc)

  • Tsukasa Kusakizako

    (The University of Tokyo)

  • Shin Hamamoto

    (The University of Tokyo
    The University of Tokyo)

  • Tomoaki Sobajima

    (University of Oxford)

  • Yuichiro Fujiwara

    (Kagawa University)

  • Keitaro Yamashita

    (The University of Tokyo
    MRC Laboratory of Molecular Biology)

  • Hisashi Kawasaki

    (The University of Tokyo
    The University of Tokyo)

  • Andrés D. Maturana

    (Nagoya University)

  • Tomohiro Nishizawa

    (The University of Tokyo
    Yokohama City University)

  • Osamu Nureki

    (The University of Tokyo)

Abstract

In the light reaction of plant photosynthesis, modulation of electron transport chain reactions is important to maintain the efficiency of photosynthesis under a broad range of light intensities. VCCN1 was recently identified as a voltage-gated chloride channel residing in the thylakoid membrane, where it plays a key role in photoreaction tuning to avoid the generation of reactive oxygen species (ROS). Here, we present the cryo-EM structures of Malus domestica VCCN1 (MdVCCN1) in nanodiscs and detergent at 2.7 Å and 3.0 Å resolutions, respectively, and the structure-based electrophysiological analyses. VCCN1 structurally resembles its animal homolog, bestrophin, a Ca2+-gated anion channel. However, unlike bestrophin channels, VCCN1 lacks the Ca2+-binding motif but instead contains an N-terminal charged helix that is anchored to the lipid membrane through an additional amphipathic helix. Electrophysiological experiments demonstrate that these structural elements are essential for the channel activity, thus revealing the distinct activation mechanism of VCCN1.

Suggested Citation

  • Tatsuya Hagino & Takafumi Kato & Go Kasuya & Kan Kobayashi & Tsukasa Kusakizako & Shin Hamamoto & Tomoaki Sobajima & Yuichiro Fujiwara & Keitaro Yamashita & Hisashi Kawasaki & Andrés D. Maturana & Tom, 2022. "Cryo-EM structures of thylakoid-located voltage-dependent chloride channel VCCN1," Nature Communications, Nature, vol. 13(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-30292-w
    DOI: 10.1038/s41467-022-30292-w
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    References listed on IDEAS

    as
    1. Veronica Kane Dickson & Leanne Pedi & Stephen B. Long, 2014. "Structure and insights into the function of a Ca2+-activated Cl− channel," Nature, Nature, vol. 516(7530), pages 213-218, December.
    2. Ute Armbruster & L. Ruby Carrillo & Kees Venema & Lazar Pavlovic & Elisabeth Schmidtmann & Ari Kornfeld & Peter Jahns & Joseph A. Berry & David M. Kramer & Martin C. Jonikas, 2014. "Ion antiport accelerates photosynthetic acclimation in fluctuating light environments," Nature Communications, Nature, vol. 5(1), pages 1-8, December.
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