A wheat HMW glutenin subunit gene reveals a highly repeated structure

Sugiyama, Takashi; Rafalski, Antoni; Peterson, David M.; Söll, Dieter

doi:10.1093/nar/13.24.8729

Cited by 150 publications

(47 citation statements)

References 13 publications

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“…The phenomenon could also result from differential splicing of introns in the mRNA of the gene controlling iBy, as reported for other genes (Rozek and Davidson, 1986). Yet, recently an alpha gliadin gene was shown not to include introns (Anderson et a!., 1984), and isolated HMW glutenin genes were shown to be devoid of introns (Forde et a!., 1985;Thompson eta!., 1985;Sugiyama et a!., 1985). iBy' might also result from an in vivo, or an in vitro (during the extraction process) proteolytic digestion of the iBy subunit, as was found in wheat-leaf-protein sub- The HMW glutenins encoded by the A genome have been studied to a much lesser extent, their genes not being usually expressed in cultivated wheats (Galili and Feldman, 1983c;Forde et a!., 1985).…”

Section: Discussionmentioning

confidence: 99%

Polymorphism and genetic control of high molecular weight glutenin subunits in wild tetraploid wheat Triticum turgidum var. dicoccoides

1988

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Polymorphism of the high molecular weight glutenin subunits was studied in 456 accessions of the wild wheat Triticum turgidum var. dicoccoides (2n = 4x = 28; genomes AABB), originating from 21 populations in Israel. A total of 50 different SDS PAGE migration patterns were observed, resulting from the combinations of 15 subunit patterns of the A genome and 24 subunit patterns of the B genome. Most migration patterns consisted of five subunits, varying between three and six. The migration patterns of the A genome had zero to three subunits-two being most common. The apparent molecular weights (MWs) of the slowest migrating subunit (114,000 to 103,500) and of the next in rate of migration (106,000 to 96,000) were highly correlated (r =0.97). Also, both subunits were either present (in most accessions) or absent. In 82.3 per cent of the accessions, the third subunit (MW 76,000 to 71,500) was absent, while in 16.9 per cent of the accessions all three subunits of the A genome were absent. The migration patterns of the B genome had one to three subunits-three being most common. The slowest migrating subunit (99,500 to 93,000) was present in almost all cases (993 per cent). The MWs of the next two subunits (90,500 to 82,000 and 86,000 to 78,000, respectively) were highly correlated (r = 0.95). Also, either both subunits were present, as in most cases (94

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Section: Discussionmentioning

confidence: 99%

Polymorphism and genetic control of high molecular weight glutenin subunits in wild tetraploid wheat Triticum turgidum var. dicoccoides

1988

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“…Their amino acid compositions (Table 2) [39] are characterized by high contents of glycine (14-19 mol %), glutamine (37-39 mol %) and proline (12-14 mol%). Genes for seven different HMW subunits have been isolated and the amino acid sequences of the encoded proteins deduced [40][41][42][43][44][45][46][47]. The proteins vary in length from 627 to 827 residues, with true Mr values of 67500 to 88 128.…”

Section: The Prolamins Of Wheat Barley and Ryementioning

confidence: 99%

The prolamin storage proteins of cereal seeds: structure and evolution

Shewry

Tatham

1990

Biochemical Journal

630

422

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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).…”

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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.

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A wheat HMW glutenin subunit gene reveals a highly repeated structure

Abstract: A wheat genomic library was screened with two synthetic oligonucleotides

Cited by 150 publications

References 13 publications

Polymorphism and genetic control of high molecular weight glutenin subunits in wild tetraploid wheat Triticum turgidum var. dicoccoides

Polymorphism and genetic control of high molecular weight glutenin subunits in wild tetraploid wheat Triticum turgidum var. dicoccoides

The prolamin storage proteins of cereal seeds: structure and evolution

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

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