4/16/2023 0 Comments Ykey es120 review![]() Post-translational modification analysis using PTM viewer predicted N-glycosylation (66%), N-terminal proteolysis (40%), and phosphorylation (32%) to be the dominant modification in the classical secretory proteins. Analysis of cuticle extract by nanoliter osmometer-phase contrast microscopy detected antifreeze activity due to non-protein component. GDSL-esterase/lipase ESM1 and β-glucanase (an antifreeze protein) showed in vitro activity. Myrosinase and its associating protein, GDSL esterase/lipase ESM1 (involved in cuticle structuring and defense) were detected in the cuticle. This system is termed as “mustard oil bomb”. Myrosinase-catalyzed glucosinolate hydrolysis releases bioactive compounds, which contribute to plant defense. Bioinformatics tool, QuickGO predicted the involvement of these proteins in catabolism (21%), peptidase activity (13%), oxidoreductase (12%), defense response (9%), fatty acid binding (9%), nutrient reservoir activity (8%), chitin binding (7%) and lipid transport (2%). Out of 615 proteins identified, 27% (169) had signal peptides supporting extracellular localization. Therefore, leaf cuticle proteins of Brassica juncea isolated using organic solvents (chloroform-methanol, 2:1(v/v)) were analyzed using gel based and quantitative shotgun proteomics. However, reports on the cuticle proteins are scanty. This lipidic layer has been explored for its cutin and wax composition. Plant cuticle, the site of perception of stress signals, is an extracellular hydrophobic barrier that covers the epidermis of the above-ground parts. Our study provides the most comprehensive analysis of dehydration-responsive secretome and the complex metabolic network operating in plant extracellular space. CaRRP1 could complement the aberrant growth phenotype of yeast mutant, deficient in vesicular transport, indicating a partial overlap of protein secretion and stress response. Its expression was positively associated with abiotic and biotic stresses. We investigated the gene structure and genomic organization and demonstrated that CaRRP1 may be involved in stress response. Screening of the secretome identified a leaderless Bet v1-like protein, designated CaRRP1, the export of which was inhibited by brefeldin A. One-third of the secreted proteins were devoid of N-terminal secretion signals suggesting a non-classical secretory route. Proteomic analysis led to the identification of 215 differentially regulated proteins, involved in a variety of cellular functions that include metabolism, cell defence, and signal transduction suggesting their concerted role in stress adaptation. Cell viability of the suspension culture remained unaltered until 96 h, which gradually declined at later stages of dehydration. ![]() ![]() To understand the underlying mechanism of stress-responsive secretion, the dehydration-responsive secretome was developed from suspension-cultured cells of chickpea. Secreted proteins maintain cell structure and biogenesis besides acting in signaling events crucial for cellular homeostasis during stress adaptation. ![]()
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