The nucleotide and deduced amino acid sequences of an HMW glutenin subunit gene from chromosome 1B of bread wheat (Triticum aestivum L.) and comparison with those of genes from chromosomes 1A and 1D

Halford, Nigel G.; Forde, J.; Anderson, Olin D.; Greene, Frank C.; Shewry, Peter R.

doi:10.1007/bf00249151

Cited by 144 publications

(75 citation statements)

References 19 publications

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“…Contig 1 contained BACs of Group 1 and Group 4, while Contig 2 was composed of BACs of the other two groups (data not shown). Previously, it has been reported that the allelic genes from the B-genome of the hexaploid bread wheat cultivar Cheyenne are 15.8 kb (Halford et al, 1987) and 20.4 kb (Anderson et al, 2002), and the Glu-A1 genes of cv Cheyenne are within 6.2 and 6.8 kb EcoRI fragments (Anderson et al, 2002). Based on the size of the four EcoRI HMW-glutenin fragments (6.1 kb, 7.0 kb, 14.6 kb, and 19.7 kb, Figure 1), and along with our previous results based on D genome substitution lines in Langdon (Cenci et al, 2003), Contig 1 with the 14.6 kb and 19.7 kb fragments represents the Glu-B1 locus, and therefore Contig 2 represents the Glu-A1 locus.…”

Section: Glu-b1 Bac Clonesmentioning

confidence: 99%

Dynamics of the evolution of orthologous and paralogous portions of a complex locus region in two genomes of allopolyploid wheat

Kong

You

et al. 2004

Plant Mol Biol

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Section: Glu-b1 Bac Clonesmentioning

confidence: 99%

Dynamics of the evolution of orthologous and paralogous portions of a complex locus region in two genomes of allopolyploid wheat

Kong

You

et al. 2004

Plant Mol Biol

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“…These sequences have revealed that these subunits contain three distinct domains, a nonrepetitive NH,-termina1 domain, a large central domain of repeated sequences, and a nonrepetitive COOH-teminal domain (Forde et al, 1985b;Sugiyama et al, 1985;Thompson, Bartels, and Harberd, 1985;Halford et al, 1987). The sequences of the HMW glutenin genes which regulate expression of the genes in the cereal endosperm are less well understood (Forde et al, 1985a).…”

Section: Introductionmentioning

confidence: 99%

Tissue-specific expression of a wheat high molecular weight glutenin gene in transgenic tobacco.

Robert¹,

Thompson²,

Flavell³

1989

Plant Cell

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“…Alleles of each of the six HMW-GS genes have been cloned and sequenced (1,8,15,28). The HMW-GS proteins coded at each Glu-J locus form two general classes, which were originally termed X-and Y-types on the basis of mobility by SDS-PAGE (22).…”

mentioning

confidence: 99%

“…The HMW-GS proteins coded at each Glu-J locus form two general classes, which were originally termed X-and Y-types on the basis of mobility by SDS-PAGE (22). The genes are thought to have diverged from a common progenitor (15).…”

mentioning

confidence: 99%

Role of the Amino- and Carboxy-Terminal Regions in the Folding and Oligomerization of Wheat High Molecular Weight Glutenin Subunits

Shani¹,

Steffen-Campbell²,

Anderson³

et al. 1992

Plant Physiol.

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The high molecular weight glutenin subunits are considered one of the most important components of wheat (Triticum aestivum) gluten, but their structure and interactions with other gluten proteins are still unknown. Understanding the role of these proteins in gluten formation may be aided by analyses of the conformation and interactions of individual wild-type and modified subunits expressed in heterologous systems. In the present report, the bacterium Escherichia coil was used to synthesize four naturally occurring X-and Y-type wheat high molecular weight glutenin subunits of the Glu-1D locus, as well as four bipartite chimeras of these proteins. Naturally occurring subunits synthesized in the bacteria exhibited sodium dodecyl sulfate-polyacrylamide gel electrophoresis migration properties identical to those of high molecular weight glutenin subunits extracted from wheat grains. Wild-type and chimeric subunits migrated in sodium dodecyl sulfate gels differently than expected based on their molecular weights due to conformational properties of their N-and C-terminal regions. Results from cycles of reductive cleavage and oxidative reformation were consistent with the formation of both inter-and intramolecular disulfide bonds in pattems and proportions that differed among specific high molecular weight glutenin species. Comparison of the chimeric and wild-type proteins indicated that the two C-terminal cysteines of the Y-type subunits are linked by intramolecular disulfide bonds, suggesting that the role of these cysteines in glutenin polymerization may be limited.The storage proteins of wheat grains (Triticum aestivum, genome AABBDD) are synthesized in the endosperm and accumulate in protein bodies inside vacuoles. Following synthesis, the storage proteins interact with each other and become incorporated into intermolecular disulfide-bonded aggregates (5). Although wheat storage proteins have been extensively studied, very little is known about their structure and interactions during protein body formation.

show abstract

The nucleotide and deduced amino acid sequences of an HMW glutenin subunit gene from chromosome 1B of bread wheat (Triticum aestivum L.) and comparison with those of genes from chromosomes 1A and 1D

Cited by 144 publications

References 19 publications

Dynamics of the evolution of orthologous and paralogous portions of a complex locus region in two genomes of allopolyploid wheat

Dynamics of the evolution of orthologous and paralogous portions of a complex locus region in two genomes of allopolyploid wheat

Tissue-specific expression of a wheat high molecular weight glutenin gene in transgenic tobacco.

Role of the Amino- and Carboxy-Terminal Regions in the Folding and Oligomerization of Wheat High Molecular Weight Glutenin Subunits

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