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Extensins are a family of flexuous, rodlike, hydroxyproline-rich glycoproteins (HRGPs) of the plant cell wall. [1] [2] They are highly abundant proteins. There are around 20 extensins in Arabidopsis thaliana. They form crosslinked networks in the young cell wall.
Hydroxyproline is found in few proteins other than collagen. For this reason, hydroxyproline content has been used as an indicator to determine collagen and/or gelatin amount. However, the mammalian proteins elastin and argonaute 2 have collagen-like domains in which hydroxyproline is formed.
Arabinogalactan-proteins (AGPs) are highly glycosylated proteins (glycoproteins) found in the cell walls of plants. Each one consists of a protein with sugar molecules attached (which can account for more than 90% of the total mass). They are members of the wider class of hydroxyproline (Hyp)-rich cell wall glycoproteins, a large and diverse ...
N-linked protein glycosylation (N-glycosylation of N-glycans) at Asn residues (Asn-x-Ser/Thr motifs) in glycoproteins. [1] Glycoproteins are proteins which contain oligosaccharide (sugar) chains covalently attached to amino acid side-chains. The carbohydrate is attached to the protein in a cotranslational or posttranslational modification.
Additionally, structural proteins (1-5%) are found in most plant cell walls; they are classified as hydroxyproline-rich glycoproteins (HRGP), arabinogalactan proteins (AGP), glycine-rich proteins (GRPs), and proline-rich proteins (PRPs). Each class of glycoprotein is defined by a characteristic, highly repetitive protein sequence.
Chlamydomonas reinhardtii is a single-cell green alga about 10 micrometres in diameter that swims with two flagella.It has a cell wall made of hydroxyproline-rich glycoproteins, a large cup-shaped chloroplast, a large pyrenoid, and an eyespot apparatus that senses light.
[2] It is a 20kDa protein whose structure is made up of beta strands forming two beta sheets to form a Greek key beta barrel with variable alpha helical structure. The copper binding domain of the protein is located at the amino-terminal end, while the carboxyl-terminal end is rich in hydroxyproline and serine residues, typical of proteins ...
Unlike systemin, it is primarily associated with the cell wall. The precursors to HypSys appear to represent a distinct subfamily of hydroxyproline-rich proteins found in cell walls. Upon wounding it is thought that a protease from the cytosol, the cell wall matrix, or the pathogen, processes the precursor producing active HypSys peptides. [13]