Recombination mapping of some chromosome 1A-, 1B-, 1D- and 6B-controlled gliadins and low-molecular-weight glutenin subunits in common wheat

Metakovsky, E. V.; Branlard, Gérard; Chernakov, V. M.; Upelniek, V. P.; Redaelli, R.; Pogna, N. E.

doi:10.1007/s001220050479

Cited by 34 publications

(18 citation statements)

References 23 publications

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“…Kasarda et al (1983) proposed that gliadins with an odd number of cysteines could form intermolecular disulfide bond and thus participate in the gluten polymer. Significant positive effects of certain gliadin alleles have been reported on gluten strength (Metakovsky et al, 1997). For example, wheats giving flour of the strong type have been found to carry gliadin blocks 1A3 (or 1A4), 1B1, 1D1 (or 1D5), 6A3, 6B1, and 6D1 (or 6D2), which are markers of high gluten quality, frost hardness, and drought resistance.…”

Section: Role Of Gliadins In Dough Rheologymentioning

confidence: 98%

“…Gliadins, one of the major gluten storage proteins of wheat, account for 40-50% of the total storage protein (Anderson et al, 1997) and confer viscous character to wheat gluten (Khatkar et al, 2002a;Wieser, 2007). Significant effects of gliadins on the gluten strength (Weegels et al, 1996;Metakovsky et al, 1997) have been reported. Past researches have suggested that gliadins may play an important role in determining the functional property of wheat flour.…”

Section: Introductionmentioning

confidence: 98%

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Biochemical and Functional Properties of Wheat Gliadins: A Review

Barak

Mudgil

Khatkar

2014

Critical Reviews in Food Science and Nutrition

134

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Gliadins account for 40-50% of the total storage proteins of wheat and are classified into four subcategories, α-, β-, γ-, and ω-gliadins. They have also been classified as ω5-, ω1, 2-, α/β-, and γ-gliadins on the basis of their primary structure and molecular weight. Cysteine residues of gliadins mainly form intramolecular disulfide bonds, although α-gliadins with odd numbers of cysteine residues have also been reported. Gliadins are generally regarded to possess globular protein structure, though recent studies report that the α/β-gliadins have compact globular structures and γ- and ω-gliadins have extended rod-like structures. Newer techniques such as Mass Spectrometry with the development of matrix-assisted laser desorption/ionization (MALDI) in combination with time-of-flight mass spectrometry (TOFMS) have been employed to determine the molecular weight of purified ω- gliadins and to carry out the direct analysis of bread and durum wheat gliadins. Few gliadin alleles and components, such as Gli-B1b, Gli-B2c and Gli-A2b in bread wheat cultivars, γ-45 in pasta, γ-gliadins in cookies, lower gliadin content for chapatti and alteration in Gli 2 loci in tortillas have been reported to improve the product quality, respectively. Further studies are needed in order to elucidate the precise role of gliadin subgroups in dough strength and product quality.

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Section: Role Of Gliadins In Dough Rheologymentioning

confidence: 98%

Section: Introductionmentioning

confidence: 98%

Biochemical and Functional Properties of Wheat Gliadins: A Review

Barak

Mudgil

Khatkar

2014

Critical Reviews in Food Science and Nutrition

134

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“…The HMW-glutenins are mapped to the Glu-1 loci on the long arm of the homoeologous group 1 chromosomes, while the LMW-glutenins are mapped to the Glu-3 loci on the short arm of the same chromosomes (Payne et al 1982;Cassidy et al 1998). Tightly linked to the Glu-3 are the Gli-1 and Gli-3 loci that encode the c-and x-gliadins, respectively (Garcia-Olmedo et al 1982;Singh and Shepherd 1988;Dubcovsky et al 1997;Metakovsky et al 1997). The a-gliadin genes are located at the Gli-2 loci of the short arm of the homoeologous group 6 chromosomes (Anderson et al 1984).…”

Section: Introductionmentioning

confidence: 98%

Rapid evolution and complex structural organization in genomic regions harboring multiple prolamin genes in the polyploid wheat genome

Gao

et al. 2007

Plant Mol Biol

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Genes encoding wheat prolamins belong to complicated multi-gene families in the wheat genome. To understand the structural complexity of storage protein loci, we sequenced and analyzed orthologous regions containing both gliadin and LMW-glutenin genes from the A and B genomes of a tetraploid wheat species, Triticum turgidum ssp. durum. Despite their physical proximity to one another, the gliadin genes and LMW-glutenin genes are organized quite differently. The gliadin genes are found to be more clustered than the LMW-glutenin genes which are separated from each other by much larger distances. The separation of the LMW-glutenin genes is the result of both the insertion of large blocks of repetitive DNA owing to the rapid amplification of retrotransposons and the presence of genetic loci interspersed between them. Sequence comparisons of the orthologous regions reveal that gene movement could be one of the major factors contributing to the violation of microcolinearity between the homoeologous A and B genomes in wheat. The rapid sequence rearrangements and differential insertion of repetitive DNA has caused the gene islands to be not conserved in compared regions. In addition, we demonstrated that the i-type LMW-glutenin originated from a deletion of 33-bps in the 5' coding region of the m-type gene. Our results show that multiple rounds of segmental duplication of prolamin genes have driven the amplification of the omega-gliadin genes in the region; such segmental duplication could greatly increase the repetitive DNA content in the genome depending on the amount of repetitive DNA present in the original duplicate region.

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“…LMW glutenins are encoded by genes present at the Glu-3 loci on the short arms of chromosomes 1A, 1B, and 1D of hexaploid wheat (Singh and Shepherd 1988). They are present as a multigene family in close association with the Gli-1 loci, encoding the γ-and ω-gliadins (Metakovsky et al 1997). The α/β-gliadins are encoded by the Gli-2 loci on the short arm of group 6 chromosomes.…”

Section: Introductionmentioning

confidence: 99%

Characterization of low-molecular-weight glutenin genes in Aegilops tauschii

et al. 2004

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This paper reports the characterization of the low-molecular-weight (LMW) glutenin gene family of Aegilops tauschii (syn. Triticum tauschii), the D-genome donor of hexaploid wheat. By analysis of bacterial artificial chromosome (BAC) clones positive for hybridization with an LMW glutenin probe, seven unique LMW glutenin genes were identified. These genes were sequenced, including their untranslated 3' and 5' flanking regions. The deduced amino acid sequences of the genes revealed four putative active genes and three pseudogenes. All these genes had a very high level of similarity to LMW glutenins characterized in hexaploid wheat. The predicted molecular weights of the mature proteins were between 32.2 kDa and 39.6 kDa, and the predicted isoelectric points of the proteins were between 7.53 and 8.06. All the deduced proteins were of the LMW-m type. The organization of the seven LMW glutenin genes appears to be interspersed over at least several hundred kilo base pairs, as indicated by the presence of only one gene or pseudogene per BAC clone. Southern blot analysis of genomic DNA of Ae. tauschii and the BAC clones containing the seven LMW glutenin genes indicated that the BAC clones contained all LMW glutenin-hybridizing bands present in the genome. Two-dimensional gel electrophoresis of an LMW glutenin extract from Ae. tauschii was conducted and showed the presence of at least 11 distinct proteins. Further analysis indicated that some of the observed proteins were modified gliadins. These results suggest that the actual number of typical LMW glutenins may in fact be much lower than previously thought, with a number of modified gliadins also being present in the polymeric fraction.

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Recombination mapping of some chromosome 1A-, 1B-, 1D- and 6B-controlled gliadins and low-molecular-weight glutenin subunits in common wheat

Cited by 34 publications

References 23 publications

Biochemical and Functional Properties of Wheat Gliadins: A Review

Biochemical and Functional Properties of Wheat Gliadins: A Review

Rapid evolution and complex structural organization in genomic regions harboring multiple prolamin genes in the polyploid wheat genome

Characterization of low-molecular-weight glutenin genes in Aegilops tauschii

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