Proteomic analysis relevant to cereal grains

Proteomics complements the analysis of gene expression by analyzing all the polypeptides (proteins) expressed by an organism's genome in a specific plant or grain tissue at a particular stage of development and under defined growth conditions. Diverse technologies have been developed for the fractionation and identification of the individual polypeptides that constitute the proteome. Information resulting from proteomics is being used to facilitate novel and conventional plant breeding

Antioxidative properties and macrochemical composition of five commercial mungbean varieties in Australia

Chandra, SS ORCiD: 0000-0002-4257-5860; Johnson, JB ORCiD: 0000-0002-9172-8587; Naiker, M ORCiD: 0000-0002-6844-8325; Power, A ORCiD: 0000-0002-7119-8486Mungbeans are growing in popularity among Australian consumers, driven by theirbeneficial nutritional and phytochemical composition. However, data on theantioxidative, mineral, and phytochemical content of Australian mungbeans at thepoint of consumer purchase remains scarce. Here, five commercial mungbean sam-ples were analysed for total antioxidant capacity, total phenolics, and total mono-meric anthocyanins. Attenuated total reflectance midinfrared spectroscopy wasutilised as a rapid and reliable method of obtaining information about the mac-rochemical composition of the mungbean hulls. Total antioxidant capacity rangedfrom 170 to 570 mg Trolox equivalents per 100 g, total phenolic content from130 to 240 mg gallic acid equivalents per 100 g, and anthocyanin content from 10 to40 mg cyanidin-3-glucoside equivalents per 100 g. There was a significant differencebetween varieties in all measures of antioxidant, phenolic and anthocyanin contents.Using principal component analysis, the midinfrared spectra for the five mungbeanvarieties could be isolated, highlighting the differences in their phytochemical compo-sition. In general, whole Australian mungbeans appear to have the highest antioxi-dant, phenolic, and anthocyanin contents. Midinfrared spectroscopy appears to be avaluable method of obtaining and comparing the macrochemical composition ofmungbeans. This technology is likely to be of increasing use in the future

Proteomic and genetic analysis of wheat endosperm albumins and globulins using deletion lines of cultivar Chinese Spring

Albumins and globulins from the endosperm of Triticum aestivum L. cv Chinese Spring (CS) were analysed to establish a proteome reference map for this standard wheat cultivar. Approximately, 1,145 Coomassie-stained spots were detected by two-dimensional gel electrophoresis (2DE), 410 of which were identified using mass spectrometry and data mining. Salt-soluble endosperm proteins from 67 CS deletion lines were also separated by 2DE (four gels per line). Image analysis of the 268 2DE gels as compared to the CS reference proteome allowed the detection of qualitative and quantitative variations in endosperm proteins due to chromosomal deletions. This differential analysis of spots allowed structural or regulatory genes, encoding 211 proteins, to be located on segments of the 21 wheat chromosomes. In addition, variance analysis of quantitative variations in spot volume showed that the expression of 391 proteins is controlled by one or more chromosome bins with 262 significant increases and 196 significant decreases in spot volume. The spot volume of several proteins was increased or decreased by numerous chromosomal regions and homoeologous-like regulation was revealed for some proteins. Quantitative or qualitative variation in a total of 386 proteins was influenced by genes assigned to at least one chromosomal region, while 66 % of all stained proteins were not found to be influenced by chromosome bins. Proteomics of deletion lines can, therefore, be used to simultaneously analyse the composition and genetics of a complex tissue, such as the wheat endosperm.Journal ArticleResearch Support, Non-U.S. Gov'tSCOPUS: ar.jinfo:eu-repo/semantics/publishe

Mapping and proteomic analysis of albumin and globulin proteins in hexaploid wheat kernels (Triticum aestivum L.)

Albumins and globulins of wheat endosperm represent 20% of total kernel protein. They are soluble proteins, mainly enzymes and proteins involved in cell functions. Two-dimensional gel immobiline electrophoresis (2DE) (pH 4-7) x SDS-Page revealed around 2,250 spots. Ninety percent of the spots were common between the very distantly related cultivars 'Opata 85' and 'Synthetic W7984', the two parents of the International Triticeae Mapping Initiative (ITMI) progeny. 'Opata' had 130 specific spots while 'Synthetic' had 96. 2DE and image analysis of the soluble proteins present in 112 recombinant inbred lines of the F9-mapped ITMI progeny enabled 120 unbiased segregating spots to be mapped on 21 wheat (Triticum aestivum L. em. Thell) chromosomes. After trypsic digestion, mapped spots were subjected to MALDI-Tof or tandem mass spectrometry for protein identification by database mining. Among the 'Opata' and 'Synthetic' spots identified, many enzymes have already been mapped in the barley and rice genomes. Multigene families of Heat Shock Proteins, beta-amylases, UDP-glucose pyrophosphorylases, peroxydases and thioredoxins were successfully identified. Although other proteins remain to be identified, some differences were found in the number of segregating proteins involved in response to stress: 11 proteins found in the modern selected cultivar 'Opata 85' as compared to 4 in the new hexaploid 'Synthetic W7984'. In addition, 'Opata' and 'Synthetic' differed in the number of proteins involved in protein folding (2 and 10, respectively). The usefulness of the mapped enzymes for future research on seed composition and characteristics is discussed