Unique lignin modifications pattern the nucleation of silica in sorghum endodermis.

08:00 EDT 10th March 2020 | BioPortfolio

Summary of "Unique lignin modifications pattern the nucleation of silica in sorghum endodermis."

Silicon oxide in the form of hydrated silica (SiO2·nH2O) is a constituent of plant tissues that in certain taxa can make several percent per dry weight. Nonetheless, the formation mechanism of plant silica is mostly unknown. Si is taken up from the soil by roots in the form of mono-silicic acid molecules (H4SiO4). The silicic acid is carried in the xylem and subsequently polymerizes in target sites to silica. In roots of sorghum (Sorghum bicolor), silica aggregates form in an orderly pattern along the inner tangential cell walls of endodermis cells. Using Raman micro-spectroscopy, auto-fluorescence and scanning electron microscopy we investigated the structure and composition of developing aggregates in roots of sorghum seedling. Putative silica aggregation loci were identified in roots grown under Si starvation. These micrometer-scale spots were constructed of tightly packed modified lignin, and nucleated trace concentrations of silicic acid. Substantial variation in cell wall auto-fluorescence between Si+ and Si- roots demonstrated the impact of Si on cell wall chemistry. We propose that in Si- roots, the modified lignin crosslinked into the cell wall and lost its ability to nucleate silica. In Si+ roots, silica polymerized on the modified lignin and altered its structure. Our work demonstrates a profound control over lignin and silica deposition in cell walls.


Journal Details

This article was published in the following journal.

Name: Journal of experimental botany
ISSN: 1460-2431


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Medical and Biotech [MESH] Definitions

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Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility.

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