scholarly journals Composition of High Molecular Weight Glutenin Subunits in Polish Common Wheat Cultivars (Triticum aestivum L.)

2018 ◽  
Vol 2018 ◽  
pp. 1-8 ◽  
Author(s):  
Ewa Filip
Keyword(s):  
Molecular Weight ◽  
Triticum Aestivum ◽  
High Molecular Weight ◽  
Wheat Gluten ◽  
Triticum Aestivum L ◽  
Glutenin Subunits ◽  
Bread Making ◽  
New Information ◽  
Sds Page ◽  
Genes Encoding

The main goal of our study was to present research data on genes encoding high molecular weight glutenin subunits (HMW-GS) associated with high flour bread-making quality. This is the leading research objective in our institute in the area of wheat gluten in cultivars that have not been studied so far in that respect, but which can potentially be a valuable source of new information. Identification and characterization of high molecular weight glutenin subunits (HMW-GS) were performed using sequencing and SDS-PAGE and STS-PCR methods. Genes located in the vicinity of the Glu-1 locus have been identified and characterized in 28 Polish cultivars of Triticum aestivum. The results were then analyzed using the following computer programs: Finch TV, BLAST, MEGA 4, Molecular Imager® Gel Doc™ XR, and Quantity One software (Bio-Rad). Three alleles (a, b, c) have been identified in the Glu-A1 locus, 6 alleles (a, b, c, d, e, k) in the Glu-B1 locus, and 2 alleles (a, d) in Glu-D1 using the SDS-PAGE method. The amplification of specific HMW-GS sequences generated one product of 450 bp in 1Dx5 in 13 cultivars of old wheat and of 435 bp in 1Dx2 in 15 cultivars. The amplification products of primers for 1Dy10 and 1Dy12 genes were 422 bp and 552 bp in size, respectively.

scholarly journals Identification of Glu-A1 and Glu-D1 High Molecular Weight Glutenin Subunits of Common Wheat (Triticum aestivum L.) Using Genetic Markers

2018 ◽  
Vol 72 (6) ◽  
pp. 349-357
Author(s):  
Marina Tikhonova ◽  
Anne Ingver ◽  
Reine Koppel
Keyword(s):  
Molecular Weight ◽  
Triticum Aestivum ◽  
High Molecular Weight ◽  
Common Wheat ◽  
Triticum Aestivum L ◽  
Glutenin Subunits ◽  
Bread Making ◽  
Accurate Identification ◽  
Sds Page ◽  
Pcr Method

Abstract High molecular weight glutenin subunits (HMW-GS) of wheat are important factors in the determination of bread-making quality. They are responsible for elasticity and polymer formation of wheat dough. In the present study, 43 winter and 40 spring common wheat (Triticum aestivum L.) cultivars originated from Estonia, Belarus, Finland, Denmark, France, Germany, the Great Britain, Latvia, Lithuania, the Netherlands, Norway, Poland, Russia, Sweden, and New Zealand were characterised for Glu-A1 and Glu-D1 allelic composition using PCR method. Analyses were conducted with one DNA marker for identification of Glu-D1 allele encoding subunit Dx5, three DNA markers for Glu-A1 Ax1, Ax2* and AxNull subunits. It was determined that 32 (74.4%) winter and 35 (83.3%) spring cultivars had allele Glu-D1d, and 23 (53.5%) winter and 33 (78.6%) spring — Glu-A1a or Glu-A1b alleles, which have positive effect on dough properties. Polymorphism at Glu-A1 locus was detected in 15 cultivars, and 9 cultivars were polymorphic for locus Glu-D1. The obtained results were compared with published SDS-PAGE data. Complete or partial agreements were found for 78.1% of Glu-A1 and 70.6% of Glu-D1 alleles. Rapid and accurate identification of wheat Glu-1 alleles by molecular markers can be used for selection of wheat genotypes with good bread-making potential.

scholarly journals Recovery of Wheat Heritage for Traditional Food: Genetic Variation for High Molecular Weight Glutenin Subunits in Neglected/Underutilized Wheat

Agronomy ◽  
2019 ◽  
Vol 9 (11) ◽  
pp. 755 ◽  
Author(s):  
Alvarez ◽  
Guzmán
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Agronomic Traits ◽  
Triticum Aestivum L ◽  
Glutenin Subunits ◽  
Traditional Foods ◽  
New Crops ◽  
Sds Page ◽  
Dwarf Wheat ◽  
End Use

Club wheat (Triticum aestivum L. ssp. compactum (Host) Mackey), macha wheat (T. aestivum L. ssp. macha (Dekapr. & A.M. Menabde) Mackey) and Indian dwarf wheat (T. aestivum L. ssp. sphaerococcum (Percival) Mackey) are three neglected or underutilized subspecies of hexaploid wheat. These materials were and are used to elaborate modern and traditional products, and they could be useful in the revival of traditional foods. Gluten proteins are the main grain components defining end-use quality. The high molecular weight glutenin subunit compositions of 55 accessions of club wheat, 29 accessions of macha wheat, and 26 accessions of Indian dwarf wheat were analyzed using SDS-PAGE. Three alleles for the Glu-A1 locus, 15 for Glu-B1 (four not previously described), and four for Glu-D1 were detected. Their polymorphisms could be a source of genes for quality improvement in common wheat, which would permit both their recovery as new crops and development of modern cultivars with similar quality characteristics but better agronomic traits.

An approach for isolating high-molecular-weight glutenin subunit genes using monoclonal antibodies

Genome ◽  
2006 ◽  
Vol 49 (2) ◽  
pp. 181-189 ◽  
Author(s):  
H Q Wang ◽  
X Y Zhang
Keyword(s):  
Molecular Weight ◽  
Monoclonal Antibody ◽  
Triticum Aestivum ◽  
Amino Acid ◽  
High Molecular Weight ◽  
Storage Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Glutenin Subunits ◽  
Sds Page

High-molecular-weight glutenin subunits (HMW-GSs) play an important role in the breadmaking quality of wheat flour. In China, cultivars such as Triticum aestivum 'Xiaoyan No. 6' carrying the 1Bx14 and 1By15 glutenin subunits usually have attributes that result in high-quality bread and noodles. HMW-GS 1Bx14 and 1By15 were isolated by preparative sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) and used as an antigen to immunize BALB/c mice. A resulting monoclonal antibody belonging to the IgG1 subclass was shown to bind to all HMW-GSs of Triticum aestivum cultivars, but did not bind to other storage proteins of wheat seeds in a Western blot analysis. After screening a complementary DNA expression library from immature seeds of 'Xiaoyan No. 6' using the monoclonal antibody, the HMW-GS 1By15 gene was isolated and fully sequenced. The deduced amino acid sequence showed an extra stretch of 15 amino acid repeats consisting of a hexapeptide and a nonapeptide in the repetitive domain of this y-type HMW subunit. Bacterial expression of a modified 1By15 gene, in which the coding sequence for the signal peptide was removed and a BamHI site eliminated, gave rise to a protein with mobility identical to that of HMW-GSs extracted from seeds of 'Xiaoyan No. 6' via SDS-PAGE. This approach for isolating genes using specific monoclonal antibody against HMW-GS genes is a good alternative to the extensively used polymerase chain reaction (PCR) technology based on sequence homology of HMW-GSs in wheat and its relatives.Key words: wheat, HMW-GS, monoclonal antibody, immunoscreen.

scholarly journals Conformational differences between two wheat (Triticum aestivum) ‘high-molecular-weight’ glutenin subunits are due to a short region containing six amino acid differences

1989 ◽  
Vol 263 (3) ◽  
pp. 837-842 ◽  
Author(s):  
A P Goldsbrough ◽  
N J Bulleid ◽  
R B Freedman ◽  
R B Flavell
Keyword(s):  
Molecular Weight ◽  
Triticum Aestivum ◽  
Amino Acid ◽  
High Molecular Weight ◽  
Polyacrylamide Gel Electrophoresis ◽  
Amino Acid Sequences ◽  
Glutenin Subunits ◽  
Sds Page ◽  
Hmw Glutenin

‘High-molecular-weight’ (HMW, high-Mr) glutenin subunits are protein constituents of wheat (Triticum aestivum) seeds and are responsible in part for the viscoelasticity of the dough used to make bread. Two subunits, numbered 10 and 12, are the products of allelic genes. Their amino acid sequences have been derived from the nucleic acid sequences of the respective genes. Subunit 10 has fewer amino acids than subunit 12, but migrates more slowly on SDS/PAGE (polyacrylamide-gel electrophoresis). This anomaly is due to between one and six of the amino acid differences between the subunits, localized towards the C-terminal end of the proteins. This has been established by making chimaeric genes between the genes for subunits 10 and 12, transcribing and translating them in vitro and analysing the products by SDS/PAGE. The postulated conformational differences between subunits 10 and 12 are discussed in relation to current hypotheses for the structure of HMW glutenin subunits.

scholarly journals Characterisation of a novel high-molecular-weight glutenin subunit 1Dy12.3 from hexaploid wheat (Triticum aestivum L.)

2012 ◽  
Vol 48 (No. 4) ◽  
pp. 157-168 ◽  
Author(s):  
D. Mihálik ◽  
E. Gregová ◽  
P. Galuszka ◽  
L. Ohnoutková ◽  
T. Klempová ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Triticum Aestivum ◽  
High Molecular Weight ◽  
Hexaploid Wheat ◽  
Signal Sequence ◽  
Triticum Aestivum L ◽  
Glutenin Subunit ◽  
Repetitive Domain ◽  
Sds Page ◽  
Methionine Residues

A novel high-molecular-weight glutenin subunit encoded by the Glu-1D locus was identified in hexaploid wheat (Triticum aestivum L.) cultivar Noe and was designated as 1Dy12.3. This subunit differed in SDS-PAGE mobility from the well-known 1Dy10 and 1Dy12 subunits that are also encoded by this locus. An analysis of the gene sequences confirmed the uniqueness of 1Dy12.3 and revealed that it is most closely related to the 1Dy12 subunit. The size of the deduced protein was calculated to be 67 884 Da, which is different from the 1Dy10 and 1Dy12 subunits (67 475 Da and 68 713 Da, respectively). The 1Dy12.3 protein consists of 652 residues, with a highly conserved signal sequence and N- and C-terminal domains, although the central repetitive domain comprising motifs of hexapeptide (PGQGQQ) and nonapeptide (GYYPTSLQQ) repeats was less conserved. The 1Dy12.3 subunit demonstrates fewer QHPEQG hexapeptide motifs and exhibits an increased number of methionine residues in comparison to the other characterised high-molecular-weight glutenin subunits. The 1Dy12.3 subunit was cloned and expressed in Escherichia coli and was detected with a prolamin-specific antibody. The size of the detected immunocomplex corresponded to the native 1Dy12.3 protein isolated from grains. The existence and characterisation of this novel high-molecular-weight glutenin subunit increases the diversity of the glutenins encoded by the Glu-1D locus.

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