Structural Basis for Silicic Acid Uptake by Higher Plants

J Mol Biol. 2021 Oct 15;433(21):167226. doi: 10.1016/j.jmb.2021.167226. Epub 2021 Sep 3.

Abstract

Many of the world's most important food crops such as rice, barley and maize accumulate silicon (Si) to high levels, resulting in better plant growth and crop yields. The first step in Si accumulation is the uptake of silicic acid by the roots, a process mediated by the structurally uncharacterised NIP subfamily of aquaporins, also named metalloid porins. Here, we present the X-ray crystal structure of the archetypal NIP family member from Oryza sativa (OsNIP2;1). The OsNIP2;1 channel is closed in the crystal structure by the cytoplasmic loop D, which is known to regulate channel opening in classical plant aquaporins. The structure further reveals a novel, five-residue extracellular selectivity filter with a large diameter. Unbiased molecular dynamics simulations show a rapid opening of the channel and visualise how silicic acid interacts with the selectivity filter prior to transmembrane diffusion. Our results will enable detailed structure-function studies of metalloid porins, including the basis of their substrate selectivity.

Keywords: NIP channel; X-ray crystal structure; aquaporin; molecular dynamics; silicic acid transport.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Aquaporins / chemistry*
  • Aquaporins / genetics
  • Aquaporins / metabolism
  • Arabidopsis / genetics
  • Arabidopsis / metabolism
  • Arabidopsis Proteins / chemistry*
  • Arabidopsis Proteins / genetics
  • Arabidopsis Proteins / metabolism
  • Binding Sites
  • Biological Transport
  • Crystallography, X-Ray
  • Diffusion
  • Gene Expression
  • Kinetics
  • Models, Molecular
  • Molecular Dynamics Simulation
  • Oryza / genetics
  • Oryza / metabolism*
  • Plant Roots / genetics
  • Plant Roots / metabolism*
  • Protein Binding
  • Protein Conformation, alpha-Helical
  • Protein Conformation, beta-Strand
  • Protein Interaction Domains and Motifs
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / metabolism
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Silicic Acid / chemistry
  • Silicic Acid / metabolism*
  • Silicon / chemistry
  • Silicon / metabolism*
  • Substrate Specificity

Substances

  • Aquaporins
  • Arabidopsis Proteins
  • NIP2;1 protein, Arabidopsis
  • Recombinant Proteins
  • Silicic Acid
  • Silicon