Characterization of low-molecular-weight glutenin subunit genes and their protein products in common wheats

Ikeda, Tatsuya; Araki, Etsuko; Fujita, Yumiko; Yano, Hiroshi

doi:10.1007/s00122-005-0131-z

Cited by 73 publications

(64 citation statements)

References 19 publications

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“…Gliadin and glutenin represent 80% of total seed storage proteins (Perron et al, 1998). Gliadins have effects on dough viscosity and glutenins contribute to dough elasticity (Ikeda et al, 2006). There are two types of glutenin, low-molecularweight (LMW) and high-molecular-weight (HMW).…”

Section: Introductionmentioning

confidence: 99%

Allelic variations of glutenin subunits and their associationwith quality traits in bread wheat genotypes

Aktaş¹,

Baloch²

2017

Turk J Agric For

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IntroductionTurkey is a major producer of wheat, with approximately 9 × 10 6 ha sown annually leading to an annual production of 20 × 10 6 t (Baloch et al., 2016). In Turkey, a national wheat breeding program was initiated in 1967, the National Wheat Release and Training Project, with the collaboration of international organizations such as the International Maize and Wheat Improvement Center (CIMMYT) and International Center for Agricultural Research in the Dry Areas (ICARDA). This program started the process of a national green revolution that resulted in an increase in wheat yield and the development of more than 100 wheat cultivars, most significantly contributing to the economy of Turkey. Nearly all the wheat cultivars in Turkey were direct or indirect input from CIMMYT and ICARDA bread wheat breeding programs that focused on increasing the quality and quantity of wheat for the developing world (Alsaleh et al., 2015(Alsaleh et al., , 2016. However, the Turkish flour industry has continued to import high-quality wheat at a high cost due to the lack of cultivars with good quality traits. Therefore, one of the main objectives of the Turkish bread wheat breeding program is to develop wheat varieties with higher grain yield (GY) and better bread-making qualities in terms of protein and gluten content (Baloch et al., 2017). In this process, it is important to consider and evaluate genotypes, environments, and their interaction as the main factors affecting wheat quality traits.The quality of bread-making is mainly related to the composition of endosperm storage proteins, namely gliadins and glutenins (Dessalegn et al., 2011). Gliadins are monomeric proteins synthesized by the Gli-1 and Gli-2 loci, which are located on the short arms of homoeologous chromosomes (He et al., 2005). Gliadin and glutenin represent 80% of total seed storage proteins (Perron et al., 1998). Gliadins have effects on dough viscosity and glutenins contribute to dough elasticity (Ikeda et al., 2006). There are two types of glutenin, low-molecularweight (LMW) and high-molecular-weight (HMW). LMW glutenin subunits are encoded by the Glu-3 loci located on the short arms of chromosomes 1A, 1B, and 1D while HMW subunits are encoded by the Glu-1 loci on chromosomes 1A, 1B, and 1D (Békés et al., 2006).

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Section: Introductionmentioning

confidence: 99%

Allelic variations of glutenin subunits and their associationwith quality traits in bread wheat genotypes

Aktaş¹,

Baloch²

2017

Turk J Agric For

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“…4B). Therefore, the LMW-GS gene of clone 4-228 belonged to Group 11 encoded by the Glu-A1 gene on chromosome 1A in Chinese Spring (Ikeda et al 2006).…”

Section: Discussionmentioning

confidence: 99%

“…X12928). A clone for the LMW-GS gene was selected by PCR using the primers Glu-4.2 (GCAACTTTGATGAT GAATCC) and Glu-5.4 (AAACAAAGGTGATCCAAC TAT) (Ikeda et al 2006). PCR was performed in a total reaction solution of 25 µl containing 1.5 mM of MgCl 2 , 0.1 mM of each dNTP, 5 pmol of each primer, 0.5 U of AmpliTaq Gold DNA polymerase (Applied Biosystems, USA), PCR Gold buffer (Applied Biosystems) and 50 ng of total DNA.…”

Section: Selection Of Wheat Tac Clones With Glutenin Subunitmentioning

confidence: 99%

Development of transgenic rice (Oryza sativa L.) expressing wheat high-and low-molecular-weight glutenin subunit proteins

et al. 2008

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We isolated transformation-competent artificial chromosome (TAC) clones harboring a high-molecularweight glutenin subunit (HMW-GS) gene and a low-molecular-weight GS (LMW-GS) gene from wheat genomic DNA, and developed transgenic rice lines with these genes using a transformation system mediated by Agrobacterium tumefaciens. We developed two lines of transgenic rice, one expressing the gene coding for HMW-GS and the other expressing the gene coding for LMW-GS. By crossing these transgenic lines, a novel line harboring both genes was developed and the expression of GS proteins was analyzed. This is the first study indicating that the two kinds of wheat GSs, HMW-GS and LMW-GS, accumulated in rice endosperm. In all the transgenic lines, the introduced GS genes were expressed in the rice endosperm, and the expressed proteins were processed at the same site as the mature GS protein in wheat seeds, forming insoluble polymeric proteins similar to those found in wheat. It was suggested that the protein-processing system was conserved between rice and wheat, and that it was possible to produce wheat gluten using the proteinprocessing system of rice.

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“…The gliadins were dissolved in 250 μl of isoelectric focusing (IEF) sample buffer containing 16% isopropanol, 8.5 M urea, 4% (w/v) CHAPS, 25 mM DTT, and 0.5% (v/v) IEF buffer (GE Healthcare UK Ltd. Buckinghamshire, England) (Ikeda et al 2006). After shaking for 30 minutes and centrifuging at 20,600g for 1 minute at room temperature, 200μl of the supernatant was applied to an Immobiline Dry-Strip pH 6-11 (GE Healthcare).…”

Section: Gliadin Extraction and 2-dimensional Polyacrylamide Gel Elecmentioning

confidence: 99%

Molecular characterization of gliadins of Chinese Spring wheat in relation to celiac disease elicitors

et al. 2018

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The wheat seed storage proteins gliadin and glutenin are encoded by multigenes.Gliadins are further classified into α-, γ-, δ-and ω-gliadins. Genes encoding α-gliadins belong to a large multigene family, whose members are located on the homoeologous group 6 chromosomes at the Gli-2 loci. Genes encoding other gliadins are located on the homoeologous group 1 chromosomes at the Gli-1 loci. Two-dimensional polyacrylamide gel electrophoresis (2-DE) was used to characterize and profile the gliadins. The gliadins in aneuploid Chinese Spring wheat lines were then compared in this study. Gliadin proteins separated into 70 spots after 2-DE and a total of 10, 10 and 16 spots were encoded on chromosomes 6A, 6B and 6D, respectively, which suggested that they were α-gliadins. Similarly, six, three and seven spots were encoded on chromosomes 1A, 1B and 1D, respectively, which indicated that they were γ-gliadins.Spots that could not be assigned to chromosomes were N-terminally sequenced and were all determined to be α-gliadins or γ-gliadins. The 2-DE profiles showed that specific α-gliadin spots assigned to chromosome 6D were lost in tetrasomic chromosome 2A lines. Furthermore, western blotting against the Glia-α9 peptide, an epitope for celiac disease (CD), suggested that α-gliadins harboring the CD epitope on chromosome 6D were absent in the tetrasomic chromosome 2A lines. Systematic 3 analysis of α-gliadins using 2-DE, quantitative RT-PCR and genomic PCR revealed that tetrasomic 2A lines carry deletion of a chromosome segment at the Gli-D2 locus. This structural alteration at the Gli-D2 locus may provide a genetic resource in breeding programs for the reduction of CD immunotoxicity.

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Characterization of low-molecular-weight glutenin subunit genes and their protein products in common wheats

Cited by 73 publications

References 19 publications

Allelic variations of glutenin subunits and their associationwith quality traits in bread wheat genotypes

Allelic variations of glutenin subunits and their associationwith quality traits in bread wheat genotypes

Development of transgenic rice (Oryza sativa L.) expressing wheat high-and low-molecular-weight glutenin subunit proteins

Molecular characterization of gliadins of Chinese Spring wheat in relation to celiac disease elicitors

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