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Structural basis for high selectivity of a rice silicon channel Lsi1

Author

Listed:
  • Yasunori Saitoh

    (Research Institute for Interdisciplinary Science, Okayama University)

  • Namiki Mitani-Ueno

    (Institute of Plant Science and Resources, Okayama University)

  • Keisuke Saito

    (Research Center for Advanced Science and Technology, The University of Tokyo
    Graduate School of Engineering, The University of Tokyo)

  • Kengo Matsuki

    (Graduate School of Natural Science and Technology, Okayama University)

  • Sheng Huang

    (Institute of Plant Science and Resources, Okayama University)

  • Lingli Yang

    (Research Institute for Interdisciplinary Science, Okayama University)

  • Naoki Yamaji

    (Institute of Plant Science and Resources, Okayama University)

  • Hiroshi Ishikita

    (Research Center for Advanced Science and Technology, The University of Tokyo
    Graduate School of Engineering, The University of Tokyo)

  • Jian-Ren Shen

    (Research Institute for Interdisciplinary Science, Okayama University
    Graduate School of Natural Science and Technology, Okayama University)

  • Jian Feng Ma

    (Institute of Plant Science and Resources, Okayama University)

  • Michihiro Suga

    (Research Institute for Interdisciplinary Science, Okayama University
    Graduate School of Natural Science and Technology, Okayama University
    Japan Science and Technology Agency, PRESTO)

Abstract

Silicon (Si), the most abundant mineral element in the earth’s crust, is taken up by plant roots in the form of silicic acid through Low silicon rice 1 (Lsi1). Lsi1 belongs to the Nodulin 26-like intrinsic protein subfamily in aquaporin and shows high selectivity for silicic acid. To uncover the structural basis for this high selectivity, here we show the crystal structure of the rice Lsi1 at a resolution of 1.8 Å. The structure reveals transmembrane helical orientations different from other aquaporins, characterized by a unique, widely opened, and hydrophilic selectivity filter (SF) composed of five residues. Our structural, functional, and theoretical investigations provide a solid structural basis for the Si uptake mechanism in plants, which will contribute to secure and sustainable rice production by manipulating Lsi1 selectivity for different metalloids.

Suggested Citation

  • Yasunori Saitoh & Namiki Mitani-Ueno & Keisuke Saito & Kengo Matsuki & Sheng Huang & Lingli Yang & Naoki Yamaji & Hiroshi Ishikita & Jian-Ren Shen & Jian Feng Ma & Michihiro Suga, 2021. "Structural basis for high selectivity of a rice silicon channel Lsi1," Nature Communications, Nature, vol. 12(1), pages 1-14, December.
    • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-26535-x
    DOI: 10.1038/s41467-021-26535-x
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    References listed on IDEAS

    as
    1. Jian Feng Ma & Kazunori Tamai & Naoki Yamaji & Namiki Mitani & Saeko Konishi & Maki Katsuhara & Masaji Ishiguro & Yoshiko Murata & Masahiro Yano, 2006. "A silicon transporter in rice," Nature, Nature, vol. 440(7084), pages 688-691, March.
    2. Kazuyoshi Murata & Kaoru Mitsuoka & Teruhisa Hirai & Thomas Walz & Peter Agre & J. Bernard Heymann & Andreas Engel & Yoshinori Fujiyoshi, 2000. "Structural determinants of water permeation through aquaporin-1," Nature, Nature, vol. 407(6804), pages 599-605, October.
    3. Haixin Sui & Bong-Gyoon Han & John K. Lee & Peter Walian & Bing K. Jap, 2001. "Structural basis of water-specific transport through the AQP1 water channel," Nature, Nature, vol. 414(6866), pages 872-878, December.
    4. Kamil Gotfryd & Andreia Filipa Mósca & Julie Winkel Missel & Sigurd Friis Truelsen & Kaituo Wang & Mariana Spulber & Simon Krabbe & Claus Hélix-Nielsen & Umberto Laforenza & Graça Soveral & Per Amstru, 2018. "Human adipose glycerol flux is regulated by a pH gate in AQP10," Nature Communications, Nature, vol. 9(1), pages 1-11, December.
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