A proteomic analysis to identify cold acclimation associated proteins in wild wheat (Triticum urartu L.)

Abstract

To gain a better understanding of cold acclimation process in wheat, we applied a 2-DE based proteomic approach to discover changes in proteome profile of a diploid wild wheat (Triticum urartu L.) during prolonged cold stress treatment. To this end, plants were grown in pots and the growing seedlings (4-leaf stage) were exposed to cold stress. After 4 weeks of cold acclimation (4-6 °C) and subsequent treatment for 12 h at -2 °C, samples were collected from control and stressed plants and were subjected to proteome pattern analysis. Among approximately 450 reproducible protein spots displayed in each given 2-DE gels, 34 proteins changed significantly in abundance in response to cold stress. Among them, 25 and 9 proteins were up and down-regulated under stress condition, respectively. Analysis by matrix-assisted laser desorption ionization time of flight/time of flight mass spectrometry coupled with non-redundant protein database search allowed the identification of 20 cold-induced proteins. Integrated proteomic and database survey resulted in identification of several cold stress related proteins such as pathogenesis related protein, cold regulated protein, cold-responsive LEA/RAB-related COR protein, oxygen-evolving enhancer protein and oxalate oxidase. The presumed functions of the identified proteins were mostly related to cold acclimation, oxidative stress and photosynthesis. The possible implications of differentially accumulated proteins in acquiring systemic tolerance to freezing stress following exposure to prolonged low temperature will be discussed.

Screening and Expression Analysis of Temperature-responsing Proteins that Can Remove Low Temperature Stagnancy of Seeds Germination of <i>Lepidium apetalum</i>

“…17 cm precast linear IPG strips (pH3-10) were chosen for the Isoelectric Focusing, sample volume was unified according to the quality of seed. Methods refer to 2-DE process of spring soybean (Glycine max L.) (Tian et al, 2015) and wild wheat (Triticum urartu L.) (Gharechahi et al, 2014), the methods were changed slightly in this study. Compared with the first and second group, screening differentially expressed proteins in the third group of seeds which removed the low-temperature germination stagnancy.…”

Identification of Winter-Responsive Proteins in Bread Wheat Using Proteomics Analysis and Virus-Induced Gene Silencing (VIGS)

“…synthesis and accumulation of cryoprotectant substances such as amino acids, sugars, and antifreeze proteins which decrease the freezing point and/or prevent ice nucleation) (2,3). Plants may also avoid freezing by delaying transition from the vegetative to the reproductive phase (4). In addition, plants can tolerate cold damage by altering expression of a gene involved in photosynthesis, carbohydrate metabolism and energetic pathways, protein metabolism and amino acid metabolism, stress response, and signal transduction (3).…”

“…Examining proteome alterations for proteins is crucial; these proteins, unlike transcripts, are direct sources of plant stress responses (16). The effect of cold on protein abundance has been studied in many plants, such as soybean, barley, wheat, Arabidopsis thaliana, rice, and tobacco (4,(17)(18)(19)(20)(21).…”

“…proteomic analysis of two winter wheat cultivars that differ in low-temperature tolerance response to abrupt low-tempera-ture stress conditions) (22). The comparison of differentially abundant proteins during cold treatment is mostly performed by conventional two-dimensional electrophoresis (2-DE) or two-dimensional differential gel electrophoresis (2D-DIGE) via MS analysis, as seen in specific tissues or organelles: for example, Arabidopsis cold-and salt-tolerant relative of Thellungiella halophila rosette leaves (15); pea roots, stems and leaves (23); rice seedlings (24); rice leaves (25); rice roots (18); and wheat leaves (4,22). Generally, these studies have observed that changes in protein abundance during cold treatment were related to abiotic stress responses (26), (e.g.…”

“…Generally, these studies have observed that changes in protein abundance during cold treatment were related to abiotic stress responses (26), (e.g. pathogenesis-related protein, cold-regulated protein, coldresponsive LEA/RAB-related COR protein, oxygen-evolving enhancer protein, and oxalate oxidase) (4).…”