Seed Storage Proteins Research Articles

Seed storage protein profiling of sulphur applicated chickpea varieties grown under rainfed condition

Seed storage protein profiling of sulphur applicated chickpea varieties grown under rainfed condition

Profiling the Seed Storage Protein Among Different Genotypes of Trigonella foenum-graecum L. (Fenugreek)

A qualitative as well as quantitative categorization of seed storage proteins profiles of 23 genotypes of Trigonella foenum- graecum L. were performed by using sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) for exploring the level of genetic discrepancy at seed storage protein level. Total soluble proteins were resolved on 10% resolving gel. A dendrogram was constructed on the basis of weight of seed storage proteins, which divide total genotypes into two groups further classified into different sub groups containing different genotypes in them. The bands obtained from gel electrophoresis can serve as a potent tool in discrimination of different genotypes on the basis of their protein content. Proteins with molecular weight 66, 43 and 35 kDa were found in all the genotypes except Fgk-76, PR, Rmt-303, PEB and Rmt-361, The 43 kDa protein band was found missing in Fgk-67, AFg-2, AM-2, AFg-4, Fgk-73, although the protein with 35 kDa weight was present in all the genotypes but not in Rmt-303 same as 63 kDa which is not present in Fgk-70 and 55 kDa protein band was found missing in Fgk-67, Afg-4 and Rmt-361.

Towards coeliac-safe bread.

SummaryGluten‐free foods cannot substitute for products made from wheat flour. When wheat products are digested, the remaining peptides can trigger an autoimmune disease in 1% of the North American and European population, called coeliac disease. Because wheat proteins are encoded by a large gene family, it has been impossible to use conventional breeding to select wheat varieties that are coeliac‐safe. However, one can test the properties of protein variants by expressing single genes in coeliac‐safe cereals like maize. One source of protein that can be considered as coeliac‐safe and has bread‐making properties is teff (Eragrostis tef), a grain consumed in Ethiopia. Here, we show that teff α‐globulin3 (Etglo3) forms storage vacuoles in maize that are morphologically similar to those of wheat. Using transmission electron microscopy, immunogold labelling shows that Etglo3 is almost exclusively deposited in the storage vacuole as electron‐dense aggregates. Of maize seed storage proteins, 27‐kDa γ‐zein is co‐deposited with Etglo3. Etglo3 polymerizes via intermolecular disulphide bonds in maize, similar to wheat HMW glutenins under non‐reducing conditions. Crossing maize Etglo3 transgenic lines with α‐, β‐ and γ‐zein RNA interference (RNAi) lines reveals that Etglo3 accumulation is only dramatically reduced in γ‐zein RNAi background. This suggests that Etglo3 and 27‐kDa γ‐zein together cause storage vacuole formation and behave similar to the interactions of glutenins and gliadins in wheat. Therefore, expression of teff α‐globulins in maize presents a major step in the development of a coeliac‐safe grain with bread‐making properties.

Identification of immunogenic epitopes of two soybean glycinin proteins in chicken

ABSTRACT Two seed storage proteins, glycinin and β-conglycinin, account for most of the proteins in soymeal, while a valuable source of protein, soybean, has also been reported to be allergenic in some animals. Glycinin and conglycinin have been reported as allergens in multiple species, including humans. Allergic responses to soy proteins are due to hypersensitivity immunological reactions upon consumption of protein. We have isolated antibodies from chicken eggs to demonstrate that chickens mount an immunogenic response to soy glycinin. All three classes of chicken immunoglobulins bound glycinin protein. We identify immunogenic regions unique to each glycinin protein that bind unique repertoires of IgA, IgM and IgY. This knowledge can be used to identify variants of immunogenic glycinin epitopes to determine the role these immunogenic sites play in the allergic response of chickens to soy protein.

Structural and antioxidant analysis of Tartary buckwheat (Fagopyrum tartaricum Gaertn.) 13S globulin.

The main component of buckwheat seed storage proteins is 13S globulin. In this study, Tartary buckwheat 13S globulin was separated and its structural features were investigated using Edman sequencing and matrix-assisted laser desorption / ionization time of flight mass spectrometry (MALDI-TOF-MS). The protective effect of its enzymatic hydrolysates against oxidative stress induced by H2 O2 was also evaluated to elucidate the antioxidant mechanism. Results showed that the isolated Tartary buckwheat 13S globulin contained one acidic and one basic subunit, which were linked by a disulfide bond. Six Tartary buckwheat active peptides were obtained from the enzymatic hydrolysates of Tartary buckwheat 13S globulin acidic subunit with a molecular weight of 38 kDa, namely Pep-1, Pep-2, Pep-3, Pep-4, Pep-5, and Pep-6. Pre-treatment of cells with Tartary buckwheat active peptides maintained the redox state balance of HepG2 cells and protected the activity of antioxidant enzymes in HepG2 cells. The Tartary buckwheat active peptides improved oxidative stress in HepG2 cells via the PPAR-α/HO-1 pathway. These results provide an insight into the antioxidant mechanism of Tartary buckwheat 13S globulin and suggest that Tartary buckwheat active peptides can be used as a functional ingredient in the food industry. © 2019 Society of Chemical Industry.

Comprehensive Analysis of the Lysine Succinylome and Protein Co-modifications in Developing Rice Seeds

Lysine succinylation has been recognized as a post-translational modification (PTM) in recent years. It is plausible that succinylation may have a vaster functional impact than acetylation because of bulkier structural changes and more significant charge differences on the modified lysine residue. Currently, however, the quantity and identity of succinylated proteins and their corresponding functions in cereal plants remain largely unknown. In this study, we estimated the native succinylation occupancy on lysine was between 2% to 10% in developing rice seeds. Eight hundred fifty-four lysine succinylation sites on 347 proteins have been identified by a thorough investigation in developing rice seeds. Six motifs were revealed as preferred amino acid sequence arrangements for succinylation sites, and a noteworthy motif preference was identified in proteins associated with different biological processes, molecular functions, pathways, and domains. Remarkably, heavy succinylation was detected on major seed storage proteins, in conjunction with critical enzymes involved in central carbon metabolism and starch biosynthetic pathways for rice seed development. Meanwhile, our results showed that the modification pattern of in vitro nonenzymatically succinylated proteins was different from those of the proteins isolated from cells in Western blots, suggesting that succinylation is not generated via nonenzymatic reaction in the cells, at least not completely. Using the acylation data obtained from the same rice tissue, we mapped many sites harboring lysine succinylation, acetylation, malonylation, crotonylation, and 2-hydroxisobutyrylation in rice seed proteins. A striking number of proteins with multiple modifications were shown to be involved in critical metabolic events. Given that these modification moieties are intermediate products of multiple cellular metabolic pathways, these targeted lysine residues may mediate the crosstalk between different metabolic pathways via modifications by different moieties. Our study exhibits a platform for extensive investigation of molecular networks administrating cereal seed development and metabolism via PTMs.

Phalaenopsis LEAFY COTYLEDON1-Induced Somatic Embryonic Structures Are Morphologically Distinct From Protocorm-Like Bodies.

Somatic embryogenesis is commonly used for clonal propagation of a wide variety of plant species. Induction of protocorm-like-bodies (PLBs), which are capable of developing into individual plants, is a routine tissue culture-based practice for micropropagation of orchid plants. Even though PLBs are often regarded as somatic embryos, our recent study provides molecular evidence to argue that PLBs are not derived from somatic embryogenesis. Here, we report and characterize the somatic embryonic tissues induced by Phalaenopsis aphrodite LEAFY COTYLEDON1 (PaLEC1) in Phalaenopsis equestris. We found that PaLEC1-induced somatic tissues are morphologically different from PLBs, supporting our molecular study that PLBs are not of somatic embryonic origin. The embryonic identity of PaLEC1-induced embryonic tissues was confirmed by expression of the embryonic-specific transcription factors FUSCA3 (FUS3) and ABSCISIC ACID INSENSITIVE3 (ABI3), and seed storage proteins 7S GLOBULIN and OLEOSIN. Moreover, PaLEC1-GFP protein was found to be associated with the Pa7S-1 and PaFUS3 promoters containing the CCAAT element, supporting that PaLEC1 directly regulates embryo-specific processes to activate the somatic embryonic program in P. equestris. Despite diverse embryonic structures, PaLEC1-GFP-induced embryonic structures are pluripotent and capable of generating new shoots. Our study resolves the long-term debate on the developmental identity of PLB and suggests that somatic embryogenesis may be a useful approach to clonally propagate orchid seedlings.

Genetic Variation for Protein Content and Yield-Related Traits in a Durum Population Derived From an Inter-Specific Cross Between Hexaploid and Tetraploid Wheat Cultivars.

Wheat grain protein content (GPC) and yield components are complex quantitative traits influenced by a multi-factorial system consisting of both genetic and environmental factors. Although seed storage proteins represent less than 15% of mature kernels, they are crucial in determining end-use properties of wheat, as well as the nutritional value of derived products. Yield and GPC are negatively correlated, and this hampers breeding programs of commercially valuable wheat varieties. The goal of this work was the evaluation of genetic variability for quantity and composition of seed storage proteins, together with yield components [grain yield per spike (GYS) and thousand-kernel weight (TKW)] in a durum wheat population obtained by an inter-specific cross between a common wheat accession and the durum cv. Saragolla. Quantitative trait loci (QTL) analysis was conducted and closely associated markers identified on a genetic map composed of 4,366 SNP markers previously obtained in the same durum population genotyped with the 90K iSelect SNP assay. A total of 22 QTL were detected for traits related to durum wheat quality. Six genomic regions responsible for GPC control were mapped on chromosomes 2B, 3A, 4A, 4B, 5B, and 7B, with major QTL on chromosomes 2B, 4A, and 5B. Nine loci were detected for GYS: two on chromosome 5B and 7A and one on chromosomes 2A, 2B, 4A, 4B, 7B, with the strongest QTL on 2B. Eight QTL were identified for TKW, three of which located on chromosome 3A, two on 1B and one on 4B, 5A, and 5B. Only small overlapping was found among QTL for GYS, TKW, and GPC, and increasing alleles coming from both parents on different chromosomes. Good candidate genes were identified in the QTL confidence intervals for GYS and TKW.

Assessment of phenotypic and storage protein diversity in exotic barley cultivated in District Dir (Pakistan)

A total of 198 exotic barley genotypes were collected from the Gene Bank of the Plant Genetic Resource Institute (PGRI), National Agriculture Research Center (NARC), Islamabad, Pakistan, for the assessment of genetic diversity based on morphological and seed storage proteins. Qualitative and quantitative traits were noted as per IPGRI, 1994 descriptor. Among the quantitative parameters, a high level of genetic variability index was noted in seeds per spike at 79.9% of coefficient of variance followed by biomass per plant which shows 37.4% variance, while minimum variance in quantitative traits was noted in days to germination at 5.4% followed by days to maturity at 3.1% with average mean genetic variation in all quantitative traits at 97.6%. Assay of total seed protein in these exotic accessions was analogue through polyacrylamide gel electrophoresis. A high level of variation was noted in loci (bands) B26 (0.98%) followed by B25 (0.89%), B24 (0.78%),B23 (0.69%) and B01 (0.52%). A similarly low level of variation was detected in B03 (0.16%) followed by B06 (0.18%), B13 (0.19%), B12 (0.21%), B11 (0.23%), B05 (0.24%), B07 (0.25%), B21 (0.34%), B20 (0.35%), B17 (0.39%). The results indicate that the mean value of variation in these accessions is 97.6%. Further assessments and exploration were suggested for these genotypes in multi-climatic zones to satisfy farmers’ need, breeders’ interest and malt-industrial requirements.

Genetic Heterogeneity of a Diploid Grass Aegilops tauschii Revealed by Chromosome Banding Methods and Electrophoretic Analysis of the Seed Storage Proteins (Gliadins)

Genetic diversity of diploid grass Ae. tauschii Coss (2n = 2x = 14, DD), the D-genome progenitor of common wheat, was assessed using fluorescence in situ hybridization (FISH) with eleven DNA probes representing satellite and microsatellite DNA sequences as well as the 45S and 5S rRNA gene families and by electrophoretic (EF) analysis of seed storage proteins (gliadins). A clear genetic differentiation of accessions into groups strangulata (Str) and tauschii (Tau) was observed. The groups differed in the presence of microsatellite repeats GAAn and ACTn and in the distribution of satellite DNA families, especially pAs1. On the basis of similarities of labeling patterns of DNA probes used in the study, we concluded that the Str group was phylogenetically closest to the D genome of common wheat. A comparison of spectra of gliadins revealed the highest similarity of Armenian and Azerbaijani accessions of Ae. tauschii to common wheat, which may indicate a contribution of Transcaucasian members of the Str group in the formation of the genetic pool of common wheat.

In-silico analysis of seed storage protein gene promoters reveals differential occurrence of 7 cis-regulatory elements in monocot and 14 in dicot plants

A major part of the human diet consists of cereals and legumes all over the world. The major dietary requirement of the developing world includes seed storage proteins of grains. However, seeds are incomplete in nutrition because of their low protein content. Synthesis of seed storage proteins is partly regulated by cis-regulatory elements (CREs) and transcription factors besides post transcriptional and post-translational level. We performed an in-silico analysis to find out significant occurrences of various cis-elements/motifs in promoters of seed storage proteins (SSPs) from 26 monocots and 28 dicot plant groups. In this paper, an in-silico analysis was performed on 1 kb region of promoters of 26 monocots and 28 dicots plant of seed storage proteins (SSPs) genes to find out the occurrences of different cis elements/motifs. Further, a statistical method was used to test the significant occurrence of motifs among a large group of the CREs/motifs. The analysis reveals differential yet significant occurrence of 7 motifs in promoters of SSPs of monocots and 14 motifs in dicots plants among 225 motifs obtained through analysis using student's t-test. The study will be helpful in designing promoters or chimeric promoter by modifying the architecture of promoters with respect to significant CREs to enhanced deposition of protein in seeds and to manipulate the seed storage oil contents.

Rice Flour: A Promising Food Material for Nutrition and Global Health.

Hunger and malnutrition, especially children, are still global issues today. Rice is a staple food for more than half of the world population and important nutritional source of not only carbohydrate but also protein. In recent aging societies, protein-energy malnutrition in elderly people emerges also as a social issue. Malnutrition in elderly people raises the risk of falling into age-related chronic diseases. Nutritional care can prevent elderly people from such age-related diseases. Rice and rice flour would be good foodstuff for preparation of diet suitable for and preferred by elderly people. Protein content of rice grains, like the other cereal grains, is less than 10% by weight, which is a little lower than meat and cheese, but higher than dairy milk and yoghurt. Nutritional quality of rice proteins is higher than the other cereal grains. Such relatively higher nutritional quality of rice proteins could be due to high copies of glutelin genes evolved from an ancestral gene common to soybean glycinin and resultant high content of legume-type seed storage proteins. Recently, rice flour became to be utilized for various processed food. The rice seed proteins as well as starch are accumulated in specific organelles termed protein bodies and amyloplast in the cells of endosperm and aleurone layer. By milling rice grains to flour particles consisting of protein and starch nanoparticles, processing characteristics of rice starch and proteins could be changed. To develop rice-based processed food for prevention of malnutrition, rice flour particles from various different rice sources could be blended for desired nutritional composition without spoiling the value of product food.

QTL analysis for relative contents of glycinin and β-conglycinin fractions from storage protein in soybean seeds under monoculture and relay intercropping

QTL analysis for relative contents of glycinin and β-conglycinin fractions from storage protein in soybean seeds under monoculture and relay intercropping

Enzymatic release of dipeptidyl peptidase-4 inhibitors (gliptins) from pigeon pea (Cajanus cajan) nutrient reservoir proteins: In silico and in vitro assessments.

In silico and in vitro parameters were used to assess the potential of pigeon pea (Cajanus cajan) nutrient reservoir proteins as sources of dipeptidyl peptidase (DPP)-4 inhibitors. In silico, 40 pigeon pea proteins evaluated had 46% of amino acids associated with DPP-4 inhibition. After virtual hydrolysis, pepsin had the highest frequency of release and bioactivity of released DPP-4 inhibiting peptides, compared to papain and thermolysin. In vitro, thermolysin released the most active DPP-4 inhibitors. The protein hydrolysates contained similar amino acids but different particle sizes. Thus, the bioactivity patterns are attributable to the different nature and behavior of proteins/peptides under actual and virtual conditions. Using eight physicochemical variables, a random forest model with moderate prediction accuracy was developed for predicting DPP-4 inhibitory activity of papain hydrolysates. The findings demonstrate that proteins from pigeon pea are precursors of DPP-4 inhibitors, with potential use in formulating functional food for managing type 2 diabetes. PRACTICAL APPLICATIONS: The emerging use of in silico simulations to predict bioactivity of peptides can provide a framework to direct further wet lab assessments. This pattern can enhance focusing on factors relevant to the bioactive properties of interest. However, there is still limited evidence to confirm the reliability and accuracy of this tool. This study therefore provides insight into the practical use of in silico simulations to predict bioactivity of food peptides by assessing the factors relevant to the enzymatic release of dipeptidyl peptidase-4 inhibitors from pigeon pea seed storage proteins and validating the findings with wet lab assessment. This work also provides important information that can enhance the utilization of pigeon pea, which is an orphan crop, in developing functional food products for managing type 2 diabetes mellitus in developing countries.

Canavanine-Induced Decrease in Nitric Oxide Synthesis Alters Activity of Antioxidant System but Does Not Impact S-Nitrosoglutathione Catabolism in Tomato Roots.

Canavanine (CAN) is a nonproteinogenic amino acid synthesized in legumes. In mammalians, as arginine analogue, it is an inhibitor of nitric oxide synthase (NOS) activity. The aim of this study was to investigate the impact of CAN-induced nitric oxide level limitation on the antioxidant system and S-nitrosoglutathione (GSNO) metabolism in roots of tomato seedlings. Treatment with CAN (10 or 50 µM) for 24–72 h led to restriction in root growth. Arginine-dependent NOS-like activity was almost completely inhibited, demonstrating direct effect of CAN action. CAN increased total antioxidant capacity and the level of sulphydryl groups. Catalase (CAT) and superoxide dismutase (SOD) activity decreased in CAN exposed roots. CAN supplementation resulted in the decrease of transcript levels of genes coding CAT (with the exception of CAT1). Genes coding SOD (except MnSOD and CuSOD) were upregulated by CAN short treatment; prolonged exposition to 50-µM CAN resulted in downregulation of FeSOD, CuSOD, and SODP-2. Activity of glutathione reductase dropped down after short-term (10-µM CAN) supplementation, while glutathione peroxidase activity was not affected. Transcript levels of glutathione reductase genes declined in response to CAN. Genes coding glutathione peroxidase were upregulated by 50-µM CAN, while 10-µM CAN downregulated GSHPx1. Inhibition of NOS-like activity by CAN resulted in lower GSNO accumulation in root tips. Activity of GSNO reductase was decreased by short-term supplementation with CAN. In contrast, GSNO reductase protein abundance was higher, while transcript levels were slightly altered in roots exposed to CAN. This is the first report on identification of differentially nitrated proteins in response to supplementation with nonproteinogenic amino acid. Among nitrated proteins differentially modified by CAN, seed storage proteins (after short-term CAN treatment) and components of the cellular redox system (after prolonged CAN supplementation) were identified. The findings demonstrate that due to inhibition of NOS-like activity, CAN leads to modification in antioxidant system. Limitation in GSNO level is due to lower nitric oxide formation, while GSNO catabolism is less affected. We demonstrated that monodehydroascorbate reductase, activity of which is inhibited in roots of CAN-treated plants, is the protein preferentially modified by tyrosine nitration.

E3 SUMO ligase AtSIZ1 regulates the cruciferin content of Arabidopsis seeds

Arabidopsis thaliana E3 SUMO ligase SIZ1 (AtSIZ1) controls vegetative growth and development, including responses to nutrient deficiency and environmental stresses. Here, we analyzed the effect of AtSIZ1 and its E3 SUMO ligase activity on the amount of seed proteins. Proteomic analysis showed that the level of three major nutrient reservoir proteins, CRUCIFERIN1 (CRU1), CRU2, and CRU3, was reduced in the siz1-2 mutant compared with the wild type. However, quantitative real-time PCR (qRT-PCR) analysis showed that transcript levels of CRU1, CRU2, and CRU3 genes were significantly higher in the siz1-2 mutant than in the wild type. Yeast two-hybrid analysis revealed direct interaction of AtSIZ1 with CRU1, CRU2, and CRU3. The sumoylation assay revealed that CRU2, and CRU3 proteins were modified with a small ubiquitin-related modifier (SUMO) by the E3 SUMO ligase activity of AtSIZ1. Additionally, high-performance liquid chromatography (HPLC) analysis showed that the amino acid content was slightly higher in siz1-2 mutant seeds than in wild type seeds. Taken together, our data indicate that AtSIZ1 plays an important role in the accumulation and stability of seed storage proteins through its E3 ligase activity.

Impact of biotechnology and nanotechnology on future bread improvement: An overview

No crop contributes more to human flesh than the wheat that gives us our daily bread. A range of products can be processed from its flour, like bread, pasta, biscuits, chapatti etc, out of which bread is the most successful one. The end use quality of bread is mainly dependent on the quality and quantity of wheat seed storage proteins. There is a continuously increasing demand for good bread products both by the consumers and baking industry. To meet the growing demand of high quality nutritious bread with long shelf life a range of biotechnical and nanotechnical formulas have been employed to bring a new shape to food for the upcoming generation. Proteomics and transformation led to improved end product by modifying the wheat seed storage proteins for improved end products. Nanotechnology is an upcoming technology which is proving to be helpful in packaging and nutritional enhancement. Here, in this article, we have listed and focused on the techniques that would be helpful in enhancing bread quality and its nutritional status in future.

Arabidopsis MDN1 Is Involved in the Establishment of a Normal Seed Proteome and Seed Germination.

Seed germination and formation are the beginning and ending, respectively, of a plant life cycle. These two processes are under fine regulation by the internal genetic information. Previously, we demonstrated that Arabidopsis MIDASIN 1 (MDN1) is required for ribosome biogenesis, and its dysfunction leads to pleiotropic developmental phenotypes, including impaired embryogenesis and slow seed germination. In this study, we further found that the weak mutant of MDN1, mdn1-1, exhibits an increased seed size phenotype. Seed proteomic analysis reveals that a number of proteins involved in seed development and response to external environments are mis-regulated by the MDN1 dysfunction. Many 2S seed storage proteins (SSPs) and late embryogenesis abundant (LEA) proteins are over-accumulated in the dry seeds of mdn1-1. Further, some genes encoding seed storage reserves are also upregulated in mdn1-1 seedlings. More interestingly, abscisic acid-insensitive 5 (ABI5) is over-accumulated in mdn1-1 seeds, and the loss of its function partially rescues the low seed germination rate of mdn1-1. Together, this study further demonstrates that MDN1 is essential for establishing a normal seed proteome, and its mutation triggers ABI5-mediated repression of seed germination.

Polymorphism of storage proteins of common backwheat (Fagopyrum esculentum Moench.) in groups of varieties with different flower color

Aim. To establish the presence of polymorphism and differences in variants of the protein spectrum of buckwheat seed storage proteins in groups of varieties with different colors of the flower corolla. Methods. Electrophoresis using the Laemmli method in 17.5% of the separating PAAG gels, visualization and identification of the spectrum variants. Results. The common variants of the electrophoretic spectrum for all groups of buckwheat varieties and the heterogeneity of each of the studied groups of genotypes are revealed. By frequency of variants of electrophoretic spectrum between groups of varieties were detected statistically significant differences and reliable predominance of individual variants in green-flower morphotypes of buckwheat were established. Conclusions. Differences in frequency of occurrence of variants of electrophoretic spectrum in different morphotypes of buckwheat indicate the probable processes of preservation of individual adaptive alleles of genes of seed storage proteins, which occurred in populations when varieties under the pressure of breeding process.
 Keywords: edible buckwheat, spare proteins, globulins, albumins, polymorphism.

Studying common wheat material from crosses with Aegilops biuncialis vis. using markers for chromosome 1U

Aim. The aim of the research was to study common wheat material developed from crosses with Aegilops biuncialis Vis. using storage protein loci as markers for chromosome 1U. Methods. SDS and APAG electrophoreses of seed storage proteins were employed to identify alleles at the Glu-1 and Gli-1 loci. The following markers of chromosome 1U of Ae. biuncialis were used: the Glu-U1 locus encoding high-molecular-weight glutenin subunits located on the long arm (1UL) and the gliadin locus Gli-U1 on the short arm (1US). Results. In F6–F7, elimination of chromosome 1U material with a frequency of about 0.222 proceeded. This indicates selection against unbalanced genotypes, which could be tracked using markers for chromosome 1U. In wheat F4–F6 hybrids from crosses with Ae. biuncialis, we revealed a high frequency of formation of genotypes possessing the 1UL arm and lacking 1US. Conclusions. Since the Glu-U1 locus on the arm 1UL encodes high-molecular-weight subunits which directly determine bread-making quality, the developed wheat material is a source of a new allele of this locus introgressed from Ae. biuncialis for enriching the common wheat gene pool. Keywords: Triticum aestivum, Aegilops biuncialis, storage proteins, introgression.