Special HMW-GSs and their genes of Triticum turgidum subsp. dicoccoides accession D141 and the potential utilization in common wheat

Guo, Xiaoyi; Hu, Jiliang; Wu, Bihua; Wang, Zhenzhen; Wang, Dong; Liu, Dengcai; Zheng, Youliang

doi:10.1007/s10722-015-0287-6

Cited by 8 publications

(10 citation statements)

References 36 publications

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“…It is sometimes possible to recover the original yield by subsequent genetic manipulation, such as backcrossing of lines with alien Glu alleles [ 53 , 54 ]. In our previous study, we revealed that the wild emmer HMW-GSs were detected in F 1 and F 2 offspring of the interspecies hybridization between common wheat and wild emmer [ 55 ]. In the current study, our strategy was to continuously select those single plants with desirable agronomic, high yield, and resistance properties for self-crossing.…”

Section: Discussionmentioning

confidence: 99%

Characterization of an Integrated Active Glu-1Ay Allele in Common Wheat from Wild Emmer and Its Potential Role in Flour Improvement

Wang

Huang

et al. 2018

IJMS

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Glu-1Ay, one of six genes encoding a high molecular weight glutenin subunit (HMW-GS), is frequently silenced in hexaploid common wheat. Here, an active allele of Glu-1Ay was integrated from wild emmer wheat (Triticum turgidum ssp. dicoccoides) accession D97 into the common wheat (Triticum aestivum) cultivar Chuannong 16 via the repeated self-fertilization of the pentaploid interspecific hybrid, culminating in the selection of a line TaAy7-40 shown to express the wild emmer Glu-1Ay allele. The open reading frame of this allele was a 1830 bp long sequence, demonstrated by its heterologous expression in Escherichia coli to encode a 608-residue polypeptide. Its nucleotide sequence was 99.2% identical to that of the sequence within the wild emmer parent. The TaAy7-40 introgression line containing the active Glu-1Ay allele showed higher protein content, higher sodium dodecyl sulfate (SDS) sedimentation value, higher content of wet gluten in the flour, higher grain weight, and bigger grain size than Chuannong 16. The end-use quality parameters of the TaAy7-40 were superior to those of the medium gluten common wheat cultivars Mianmai 37 and Neimai 9. Thus, the active Glu-1Ay allele might be of potential value in breeding programs designed to improve wheat flour quality.

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Section: Discussionmentioning

confidence: 99%

Characterization of an Integrated Active Glu-1Ay Allele in Common Wheat from Wild Emmer and Its Potential Role in Flour Improvement

Wang

Huang

et al. 2018

IJMS

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“…28,29 In addition, research has revealed that increased length of repetitive domain, a number of cysteine residues and coils would benefit the formation of gluten polymer. 22,[29][30][31] Protein secondary structure prediction of HMWGAx demonstrates that the number of the α-helixes and their position is similar to the good flour quality Ax1type HMW glutenin subunit. Moreover, HMWGAx protein contained 34% of glutamine residues, indicating the capacity to form inter-chain hydrogen bonds that could provide the elasticity for the dough.…”

Section: Discussionmentioning

confidence: 94%

Cloning and characterization of high molecular weight glutenin gene from Triticum aestivum cultivar Dacke

et al. 2018

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Background: High molecular weight (HMW) glutenin protein plays a crucial role in determining dough viscoelastic properties that determines the quality of wheat flour. The aim of the present study was to isolate, clone and analyze (in silico) the HMW glutenin gene of Triticum aestivum cultivar Dacke.Methods: Primers were designed to amplify a 2445 bp fragment of HMW glutenin gene. Ax type HMW glutenin gene from Triticum aestivum cultivar Dacke was isolated using PCR and it was sequenced by primer walking. Results: Amplified HMW glutenin gene was designated as HMWGAx. Sequence analysis revealed a complete open reading frame encoding 815 amino acid residues with N- and C terminal non-repetitive domain and a central repetitive domain. The calculated molecular weight of the deduced HMW glutenin protein was ~88 kDa and the number of cysteine residues in the HMWGAx was four, in accordance with other x type HMW glutenin proteins. Phylogenetic analysis revealed 100% homology to the previously studied Ax2* type HMW glutenin gene from cultivar Cheyenne. Predicted secondary structure results showed that it was similar to1Ax1 type of common wheat (Triticum aestivum), having superior flour milling quality.Conclusions: Sequence analysis suggests that HMWGAx protein significantly and positively correlates with the properties of elasticity and extensibility of gluten.

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“…In addition, Gli2-AT-107 contained the highest ratio of amino acid residues, which further generated the secondary structures, implying that this gene could be favorable for constructing a good gluten structure and exhibiting superior dough quality. 40,41 Based on such recognition, the quantity and distribution of the 4 toxic epitopes could be applied to associate α-gliadins with a specific chromosome. 13,15 To be specific, the α-gliadins from chromosome 6B were identified free of any intact T cell epitopes.…”

Section: ■ Discussionmentioning

confidence: 99%

“…These α-gliadin genes may be exploited as potential resources for decreasing and preventing celiac diseases. In addition, Gli2-AT-107 contained the highest ratio of amino acid residues, which further generated the secondary structures, implying that this gene could be favorable for constructing a good gluten structure and exhibiting superior dough quality. , …”

Section: Discussionmentioning

confidence: 99%

Molecular Characterization and Variation of the Celiac Disease Epitope Domains among α-Gliadin Genes in Aegilops tauschii

Liang

Bai

et al. 2017

J. Agric. Food Chem.

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To explore the distribution and quantity of toxic epitopes in α-gliadins from Aegilops tauschii, a total of 133 complete α-gliadin coding sequences were obtained, including 69 pseudogenes with at least one premature stop codon and 64 genes with complete open reading frames (ORFs). Plenty of deletions and single amino acid substitutions were found in the 4 celiac disease (CD) toxic epitope domains through multiple alignments, in which the sequence of DQ2.5-glia-α2 demonstrated the most significant changes. Interestingly, 7 of the 59 α-gliadins were free of any kind of intact CD toxic epitopes, providing potential gene resources for low CD toxicity breeding of common wheat. Analysis of the neighbor-joining tree demonstrates that 2 of the totally 7 α-gliadins cluster within the homologues of Triticum (A genome), and the other 5 group with those of Aegilops Sitopsis (B genome). This result implies that the 7 α-gliadin genes may be originated from the ancestor species of Ae. tauschii, evolved by the homoploid hybrid of Triticum and Aegilops Sitopsis. The remaining 52 α-gliadins form a separate clade from other homologues of A and B genomes, suggesting a recent rapid gene expansion by gene duplication associated with the species adaptation.

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Special HMW-GSs and their genes of Triticum turgidum subsp. dicoccoides accession D141 and the potential utilization in common wheat

Cited by 8 publications

References 36 publications

Characterization of an Integrated Active Glu-1Ay Allele in Common Wheat from Wild Emmer and Its Potential Role in Flour Improvement

Characterization of an Integrated Active Glu-1Ay Allele in Common Wheat from Wild Emmer and Its Potential Role in Flour Improvement

Cloning and characterization of high molecular weight glutenin gene from Triticum aestivum cultivar Dacke

Molecular Characterization and Variation of the Celiac Disease Epitope Domains among α-Gliadin Genes in Aegilops tauschii

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