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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.

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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

The most abundant natural aromatic organic polymer found in all vascular plants. Lignin together with cellulose and hemicellulose are the major cell wall components of the fibers of all wood and grass species. Lignin is composed of coniferyl, p-coumaryl, and sinapyl alcohols in varying ratios in different plant species. (From Merck Index, 11th ed)

A copper-containing oxidoreductase enzyme that catalyzes the oxidation of 4-benzenediol to 4-benzosemiquinone. It also has activity towards a variety of O-quinols and P-quinols. It primarily found in FUNGI and is involved in LIGNIN degradation, pigment biosynthesis and detoxification of lignin-derived products.

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A family of alpha- KETOGLUTARIC ACID and Fe(II)-dependent dioxygenases that are homologous to AlkB, an enzyme that repairs alkylated nucleic acids in E. coli. The mammalian homologs have diverse substrate specificities and functions that include DNA REPAIR, generating unique wobble modifications in URIDINE tRNA, demethylation of nucleotides in DNA and RNA, and demethylation of LYSINE residues on certain proteins, including ACTIN and histones (HISTONE CODE).

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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