Isolation and partial characterization of wheat-germ-agglutinin-like lectins from rye (Secale cereale) and barley (Hordeum vulgare) embryos.
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ABSTRACT:
SUBMITTER: Peumans WJ
PROVIDER: S-EPMC1158215 | biostudies-other | 1982 Apr
REPOSITORIES: biostudies-other
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Project description:The use of cereal microgreens is increasing because of increased consumer's interest in healthier products. Chlorophyll (Chl) and Carotenoids (Car) are suggested to correlate with health promoting components like phenolics and antioxidant potential of the plant-part. They also play role against clinical conditions like thalassemia and hemolytic anemia and reduce the risk of some chronic diseases, such as cancer, cardiovascular diseases, skin diseases and age-related eye diseases. This study was carried out for the comprehensive profiling of Chl and Car in wheat (Triticum aestivum L.), and barley (Hordeum vulgare L.) micro-greens between 7 and 16 days on dry basis. Chl and Car content strongly correlated with the number of days of growth. Significantly high correlations existed among Chl a, Chl b, total Chl and total Car with concomitant Chl a/b and Chl/Car ratios. The peaks for the rate of accumulation of pigments were between 7-10 days on wheat and 10-13 days on barley. The maximum content of Chl and Car were 616.63?±?18.45 mg/100 g DM and 54.80?±?1.72 mg/100 g DM on day 16 and statistically not significant to variety of grain. The Chl level was slightly lower than Chl rich vegetables like kale and comparable to spinach and Car level was comparable to carrots, which is higher than most of the daily consumable fruits and vegetables. Further cell-based or in vivo studies of cereal microgreens could be considered to draw more valuable information related to human health.
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Project description:Gene expression in plastids of higher plants is dependent on two different transcription machineries, a plastid-encoded bacterial-type RNA polymerase (PEP) and a nuclear-encoded phage-type RNA polymerase (NEP), which recognize distinct types of promoters. The division of labor between PEP and NEP during plastid development and in mature chloroplasts is unclear due to a lack of comprehensive information on promoter usage. Here we present a thorough investigation into the distribution of PEP and NEP promoters within the plastid genome of barley (Hordeum vulgare L). Using a novel differential RNA sequencing approach, which discriminates between primary and processed transcripts, we obtained a genome-wide map of transcription start sites in plastids of mature first leaves. PEP-lacking plastids of the albostrians mutant allowed for the unambiguous identifications of NEP promoters. We observed that the chloroplast genome contains many more promoters than genes. According to our data, most genes (including genes coding for photosynthesis proteins) have both PEP and NEP promoters. We also detected numerous transcription start sites within operons indicating transcriptional uncoupling of genes in polycistronic gene clusters. Moreover, we mapped many transcription start sites in intergenic regions, as well as opposite to annotated genes demonstrating the existence of numerous non-coding RNA candidates.
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Project description:Wheat germ agglutinin (WGA) is emblematic of proteins that specialize in the recognition of carbohydrates. It was the first lectin reported to have a capacity for discriminating between normal and malignant cells. Since then, it has become a preferred model for basic research and is frequently considered in the development of biomedical and biotechnological applications. However, the molecular basis for the structural stability of this homodimeric lectin remains largely unknown, a situation that limits the rational manipulation and modification of its function. In this work we performed a thermodynamic characterization of WGA folding and self-association processes as a function of pH and temperature by using differential scanning and isothermal dilution calorimetry. WGA is monomeric at pH 2, and one of its four hevein-like domains is unfolded at room temperature. Under such conditions, the agglutinin exhibits a fully reversible thermal unfolding that consists of three two-state transitions. At higher pH values, the protein forms weak, nonobligate dimers. This behavior contrasts with that observed for the other plant lectins studied thus far, which form strong, obligate oligomers, indicating a distinctly different molecular basis for WGA function. For dimer formation, the four domains must be properly folded. Nevertheless, depending on the solution conditions, self-association may be coupled with folding of the labile domain. Therefore, dimerization may proceed as a rigid-body-like association or a folding-by-binding event. This hybrid behavior is not seen in other plant lectins. The emerging molecular picture for the WGA assembly highlights the need for a reexamination of existing ligand-binding data in the literature.
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