The wheat γ-gliadin genes: characterization of ten new sequences and further understanding of γ-gliadin gene family structure

Anderson, Olin D.; Hsia, Chien-Chung; Torres, Villalobos

doi:10.1007/s00122-001-0551-3

Cited by 76 publications

(60 citation statements)

References 29 publications

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“…There are from 25 to 150 copies of the genes that encode the α-gliadins, depending on the variety (Anderson and Greene 1997). The γ-gliadins and ω-gliadins are encoded by clusters of gene families, composed of 15-40 and 15-18 copies, respectively (Sabelli and Shewry 1991;Anderson et al 2001). Comparisons of amino acid sequences deduced from DNA sequences have demonstrated that α-and β-gliadins have similar sequences, leading to the proposal that they be combined, so that the gliadins would be subdivided into α, γ, and ω groups ( Fig.…”

Section: Primary Structures Of Gliadinsmentioning

confidence: 99%

Gliadins from wheat grain: an overview, from primary structure to nanostructures of aggregates

2017

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Gliadins are well-known wheat grain proteins, particularly important in food science. They were studied as early as the 1700s. Despite their long history, it has been difficult to identify their higher-order structure as they aggregate in aqueous solution. Consequently, most studies have been performed by extracting the proteins in 70% ethanol or dilute acidic solutions. The carboxy-terminal half of α-and γ-gliadins have α-helix-rich secondary structures stabilized with intramolecular disulfide bonds, which are present in either aqueous ethanol or pure water. The amino-terminal-repeat region of α-and γ-gliadins has poly-Lproline II and β-reverse-turn structures. ω-Gliadins also have poly-L-proline II and β-reverse-turn structures, but no α-helix structure. The size and shape of gliadin molecules have been determined by assessing a variety of parameters: their sedimentation velocity in the analytical ultracentrifuge, intrinsic viscosity, small-angle X-ray scattering profile, and images of the proteins from scanning probe microscopes such as a tunneling electron microscope and atomic force microscope. Models for gliadins are either rods or prolate ellipsoids whether in aqueous ethanol, dilute acid, or pure water. Recently, gliadins have been shown to be soluble in pure water, and a novel extraction method into pure water has been established. This has made it possible to analyze gliadins in pure water at neutral pH, and permitted the characterization of hydrated gliadins. They formed hierarchical nanoscale structures with internal density fluctuations at high protein concentrations.

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Section: Primary Structures Of Gliadinsmentioning

confidence: 99%

Gliadins from wheat grain: an overview, from primary structure to nanostructures of aggregates

2017

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“…Therefore, these three clones are probably pseudogenes, as do two other clones (Hn4 and Hn5) from hull-less barley [18]. So far, only two B-hordein pseudogenes have been reported in other barley accessions [10,17], but pseudogenes are very common in other cereal prolamin gene families, such as those in wheat and maize [22,[26][27][28][29][30][31][32].…”

Section: Pseudogenesmentioning

confidence: 94%

Sequences variation and classification of B-hordein genes in hull-less barley from the Qinghai-Tibet Plateau

Han

Qian

et al. 2008

Mol Biol

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-The goal of this study is to understand the evolution relationship of the members of the B-hordein gene family in hull-less barley by analysis of their structure and to explore their utility in grain quality improvement. Six copies of the B-hordein gene ( Hn1 -Hn3 , Hn7 -Hn9 ) were cloned from six hull-less barley cultivars collected from Qinghai-Tibet Plateau and molecularly characterized. Comparison of their predicted polypeptide sequences with the published data suggested that they all share the same basic protein structures. In addition, we found that the C-terminal end sequences of all B-hordeins shared a similar feature. In the six clones and the other three published genes ( Hn4 , Hn5 , and Hn6 ) from hull-less barley, Hn2 and Hn7 contained the identical C-terminal end sequence DIMPVDFWH. Hn3, Hn4, Hn5, Hn8 and Hn9 also shared the common sequence DIMPPDFWH, which was similar to that of a B-hordein reported previously. Both Hn1 and Hn6 exhibited differences in their C-terminal end sequences, and they clustered into different subgroups. The B-hordeins with identical C-terminal end sequences were clustered into the same subgroup, so we believe that B-hordein gene subfamilies possibly can be classified on the basis of the conserved C-terminal end sequences of predicted polypeptide. Phylogenetic analysis also indicated that there is a relatively weak identity between our predicted B-hordeins and those reported from H. chilense and H. brevisubulatum. All of our nine predicted B-hordeins were clustered together and other B-hordeins formed another cluster. The possible use of these genes in relation to barley quality is discussed.

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“…In this research, phylogenetic analysis was performed on γ-gliadin amino acid sequences to construct a cladogram using Triticeae representative amino acid sequences as controls. The repetitive regions of γ-gliadin consist of a long direct repeat and evolve rapidly, so they are not considered suitable for determining relatedness (Anderson et al, 2001). Therefore, the repetitive domains are not included here for constructing the cladogram.…”

Section: Phylogenetic Analysis Of the Dasypyrum γ-Gliadin Genesmentioning

confidence: 99%

“…The α-and β-subfamilies are clustered on the short arms of homologous group 6 chromosomes, while γ-and ω-subfamilies are located on the short arms of homologous group 1 chromosomes (Dubcovsky et al, 1997). The γ-gliadins have been considered to be the most ancient members of the wheat glutenin (Anderson et al, 2001). The molecular cloning and sequencing of these genes are helpful for better understanding the relationships of their structures and functions, and will provide vital information on gene evolution (Guo et al, 2010).…”

Section: Introductionmentioning

confidence: 99%

“…The molecular cloning and sequencing of these genes are helpful for better understanding the relationships of their structures and functions, and will provide vital information on gene evolution (Guo et al, 2010). In the Triticeae, γ-gliadin genes have been cloned from the genus Triticum (Anderson et al, 2001;Qi et al, 2009;Altenbach et al, 2010), Aegilops (Qi et al, 2009;Huang et al, 2010), Thinopyrum , and Crithopsis (Guo et al, 2010). However, no γ-gliadin genes have been cloned from the genus Dasypyrum.…”

Section: Introductionmentioning

confidence: 99%

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Isolation and phylogenetic analysis of novel γ-gliadin genes in genus Dasypyrum

Liu²,

Yang³

et al. 2013

Genet. Mol. Res.

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ABSTRACT.As the most ancient member of the wheat gluten family, the γ-gliadin genes are suitable for phylogenetic analysis among wheat and related species. Species in the grass genus Dasypyrum have been widely used for wheat cross breeding. However, the genomic relationships among Dasypyrum species have been little studied. We isolated 22 novel γ-gliadin gene sequences, among which 10 are putatively functional. The open reading frame lengths of these sequences range from 642 to 933 bp, and these putative proteins consist of five domains. Phylogenetic analyses showed that all Dasypyrum γ-gliadin gene sequences clustered in a large group; D. villosum and tetraploid D. breviaristatum γ-gliadin gene sequences clustered in a subgroup, while diploid D. breviaristatum γ-gliadin gene sequences clustered at the edge of the subgroup. All of the Dasypyrum γ-gliadin gene sequences were absent in three major T cell-stimulatory epitopes binding to HLA-DQ2/8 in celiac disease patients. Based on the phylogenetic analyses, we suggest that D. villosum and tetraploid D. breviaristatum evolved in parallel from a diploid ancestor D. breviaristatum.

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The wheat γ-gliadin genes: characterization of ten new sequences and further understanding of γ-gliadin gene family structure

Cited by 76 publications

References 29 publications

Gliadins from wheat grain: an overview, from primary structure to nanostructures of aggregates

Gliadins from wheat grain: an overview, from primary structure to nanostructures of aggregates

Sequences variation and classification of B-hordein genes in hull-less barley from the Qinghai-Tibet Plateau

Isolation and phylogenetic analysis of novel γ-gliadin genes in genus Dasypyrum

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