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

2019 ◽  
Vol 25 ◽  
pp. 55-59
Author(s):  
N. A. Kozub ◽  
I. A. Sozinov ◽  
H. Ya. Bidnyk ◽  
N. A. Demianova ◽  
O. I. Sozinova ◽  
...  
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Common Wheat ◽  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Bread Making ◽  
Wheat Gene ◽  
The Common ◽  
Gli 1

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.

Molecular cloning, sequencing, and chromosome mapping of a 1A-encoded ω-type prolamin sequence from wheat

Genome ◽  
2002 ◽  
Vol 45 (4) ◽  
pp. 661-669 ◽  
Author(s):  
Ali Masoudi-Nejad ◽  
Shuhei Nasuda ◽  
Akira Kawabe ◽  
Takashi R Endo
Keyword(s):  
Storage Proteins ◽  
Protein Structures ◽  
Seed Storage ◽  
Chromosome Mapping ◽  
Seed Storage Proteins ◽  
Gene Families ◽  
Start Codon ◽  
Pcr Analysis ◽  
Bread Making ◽  
Deletion Lines

Gliadins are the most abundant component of the seed storage proteins in cereals and, in combination with glutenins, are important for the bread-making quality of wheat. They are divided into four subfamilies, the α-, β-, γ-, and ω-gliadins, depending on their electrophoresis pattern, chromosomal location, and DNA and protein structures. Using a PCR-based strategy we isolated and sequenced an ω-gliadin sequence. We also determined the chromosomal subarm location of this sequence using wheat aneuploids and deletion lines. The gene is 1858 bp long and contains a coding sequence 1248 bp in length. Like all other gliadin gene families characterized in cereals, the ω-gliadin gene described here had characteristic features including two repeated sequences 300 bp upstream of the start codon. At the DNA level, the gene had a high degree of similarity to the ω-secalin and C-hordein genes of rye and barley, but exhibited much less homology to the α- and β-gliadin gene families. In terms of the deduced amino acid sequence, this gene has about 80 and 70% similarity to the ω-secalin and C-hordein genes, respectively, and possesses all the features reported for other gliadin gene families. The ω-gliadin gene has about 30 repeats of the core consensus sequences PQQPX and XQQPQQX, twice as many as other gliadin gene families. Southern blotting and PCR analysis with aneuploid and deletion lines for the short arm of chromosome 1A showed that the ω-gliadin was located on the distal 25% of the short arm of chromosome 1A. By comparison of PCR and A-PAGE profiles for deletion stocks, its genomic location must be at a different locus from gli-A1a in 'Chinese Spring'.Key words: glutenin, omega gliadin, storage protein, Triticum aestivum, secalin.

Diversity of seed storage proteins in common wheat (Triticum aestivum L.)

2011 ◽  
Vol 9 (2) ◽  
pp. 256-259
Author(s):  
Zuzana Šramková ◽  
Edita Gregová ◽  
Svetlana Šliková ◽  
Ernest Šturdík
Keyword(s):  
Triticum Aestivum ◽  
Common Wheat ◽  
Gel Electrophoresis ◽  
Storage Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Triticum Aestivum L ◽  
Polyacrylamide Gel

The objective of our study was to determine the composition of high-molecular weight-glutenin subunits (HMW-GS) in 120 cultivars of common wheat (Triticum aestivum L.). Fourteen alleles and 34 allelic compositions were detected using sodium dodecyl sulphate-polyacrylamide gel electrophoresis. The most frequent HMW-GS alleles at the Glu-A1, Glu-B1 and Glu-D1 loci were null (57.1%), 7+9 (43.3%) and 5+10 (61.9%), respectively. However, low-frequency HMW-GS alleles were also observed, such as 13+16, 20, 21, 7 and 18, encoded by the Glu-B1 locus, and 4+12, encoded by the Glu-D1 locus. The wheat–rye 1BL.1RS translocation was identified in 25 cultivars, using acid polyacrylamide gel electrophoresis. The Glu-score varied greatly, and some lines reached the maximum value of 10.

Complementary Effect of High Molecular Weight Glutenin Subumits on Bread-Making Quality in Common Wheat

2009 ◽  
Vol 35 (8) ◽  
pp. 1379-1385 ◽  
Author(s):  
Yu-Shuang YANG ◽  
Bin-Shuang PANG ◽  
Lan-Fen WANG ◽  
Xue-Yong ZHANG ◽  
Yuan-Jie YU
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Common Wheat ◽  
Bread Making ◽  
Complementary Effect

scholarly journals Genetic Diversity of High and Low Molecular Weight Glutenin Subunits in Algerian Aegilops geniculata

2014 ◽  
Vol 42 (2) ◽  
pp. 453-459 ◽  
Author(s):  
Asma MEDOURI ◽  
Inès BELLIL ◽  
Douadi KHELIFI
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Storage Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Low Molecular Weight ◽  
Glutenin Subunits ◽  
Bread Making ◽  
Aegilops Geniculata ◽  
Wide Range

Aegilops geniculata Roth is an annual grass relative to cultivated wheat and is widely distributed in North Algeria. Endosperm storage proteins of wheat and its relatives, namely glutenins and gliadins, play an important role in dough properties and bread making quality. In the present study, the different alleles encoded at the four glutenin loci (Glu-M1, Glu-U1, Glu-M3 and Glu-U3) were identified from thirty five accessions of the tetraploid wild wheat A. geniculata collected in Algeria using Sodium dodecyl Sulfate - Polyacrylamide Gel Electrophoresis (SDS-PAGE). At Glu-M1 and Glu-U1 loci, encoding high molecular weight glutenin subunits (HMW-GS) or A-subunits, 15 and 12 alleles were observed respectively, including one new subunit. B-Low molecular weight glutenin subunits zone (B-LMW-GS) displayed a far greater variation, as 28 and 25 alleles were identified at loci Glu-M3 and Glu-U3 respectively. Thirty two subunits patterns were revealed at the C subunits- zone and a total of thirty four patterns resulted from the genetic combination of the two zones (B- and C-zone). The wide range of glutenin subunits variation (high molecular weight glutenin subunits and low molecular weight glutenin subunits) in this species has the potential to enhance the genetic variability for improving the quality of wheat./span>

Positive effect of the high-molecular-weight glutenin allele, Glu-D1d, on the bread-making quality of common wheat

2003 ◽  
Vol 122 (3) ◽  
pp. 279-280 ◽  
Author(s):  
H. Tanaka ◽  
N. Nakata ◽  
M. Osawa ◽  
M. Tomita ◽  
H. Tsujimoto ◽  
...  
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Common Wheat ◽  
Bread Making ◽  
Positive Effect

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

2019 ◽  
Vol 24 ◽  
pp. 92-97
Author(s):  
Y. V. Zaika ◽  
N. A. Kozub ◽  
I. A. Sozinov ◽  
G. Ya. Bidnyk ◽  
P. P. Karazhbey
Keyword(s):  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Flower Color ◽  
Fagopyrum Esculentum ◽  
Frequency Of Occurrence ◽  
Common Variants ◽  
The Common ◽  
Fagopyrum Esculentum Moench ◽  
Electrophoretic Spectrum

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.

scholarly journals Identification and Characterization of the Seed Storage Proteins and Related Genes of Cannabis sativa L.

2021 ◽  
Vol 8 ◽  
Author(s):  
Xin Sun ◽  
Yao Sun ◽  
Yao Li ◽  
Qiong Wu ◽  
Lei Wang
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Storage Protein ◽  
Cannabis Sativa ◽  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Hemp Seed ◽  
Abundant Protein ◽  
Molecular Weights

Hemp (Cannabis sativa L.) seed is emerging as a novel source of plant protein owing to its rich protein content and reasonable nutritional structure. In the current study, the storage proteins of hemp seed were extracted using different methods. The modified Osborne method yielded maximum extraction of the hemp seed storage proteins, while degreasing had little effect on the hemp seed protein (HSP) extraction. Protein identification results revealed that 11S globulin (edestin) was the most abundant protein in hemp seed, and the molecular weights of the two subunits of this protein were ~35 and 20 kDa, respectively. The second most abundant protein was 2S albumin (Cs2S), with a molecular weight of ~14–15 kDa. The least abundant protein was 7S vicilin-like protein (Cs7S), with a molecular weight of ~47 kDa. Subsequently, gene families encoding these three storage protein classes, including three genes for edestin, two for Cs2S, and one for Cs7S, were cloned and then analyzed for amino acid composition and structure. The three edestins were different in their amino acid sequences and calculated molecular weights. The analysis of coding sequences revealed a higher percentage of similarity (62.7%) between Edestin1 and Edestin3, while the similarity decreased significantly to ~57% between Edestin1 and Edestin2, and 58% between Edestin2 and Edestin3. The calculated protein molecular weight was the highest for the protein encoded by Edestin1 and the smallest for the protein encoded by Edestin2. All three edestins were rich in arginine, while Edestin3 had a higher methionine content relative to that in the other two, which proved that Edestin3 had a better nutritional value. Cs2S and Cs7S were different from those reported in previous studies. Therefore, it could be inferred that amino acid composition varies with different hemp cultivars. The current research brought significant theoretical advance in illuminating the understanding of hemp seed storage protein and would have significance for future research on improving the nutritional quality of hemp seed and developing bioactive peptides.

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