2021年10月29日
Structural basis for high selectivity of a rice silicon channel Lsi1
Nature Communications
- 巻
- 12
- 号
- 1
- 開始ページ
- 6236
- 終了ページ
- 6236
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1038/s41467-021-26535-x
- 出版者・発行元
- 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.
- リンク情報
-
- DOI
- https://doi.org/10.1038/s41467-021-26535-x
- PubMed
- https://www.ncbi.nlm.nih.gov/pubmed/34716344
- PubMed Central
- https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8556265
- 共同研究・競争的資金等の研究課題
- 穀物由来ケイ酸チャネルの基質選択機構の解明
- 共同研究・競争的資金等の研究課題
- 穀物アクアポリンのケイ酸取り込み機構の解明
- URL
- https://www.nature.com/articles/s41467-021-26535-x.pdf
- URL
- https://www.nature.com/articles/s41467-021-26535-x
- ID情報
-
- DOI : 10.1038/s41467-021-26535-x
- eISSN : 2041-1723
- PubMed ID : 34716344
- PubMed Central 記事ID : PMC8556265