Papers

Dec, 2021

Structural basis for high selectivity of a rice silicon channel Lsi1

Nature Communications
  • 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
  • Display all

Volume
12
Number
1
Language
Publishing type
Research paper (scientific journal)
DOI
10.1038/s41467-021-26535-x
Publisher
Springer Science and Business Media LLC

<title>Abstract</title>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.

Link information
DOI
https://doi.org/10.1038/s41467-021-26535-x
URL
https://www.nature.com/articles/s41467-021-26535-x.pdf
URL
https://www.nature.com/articles/s41467-021-26535-x
ID information
  • DOI : 10.1038/s41467-021-26535-x
  • eISSN : 2041-1723

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