Identification, Cloning and Characterisation of a HMW-Glutenin Gene from an Old Hungarian Wheat Variety, Bánkúti 1201

Juhász, Angéla; Tamás, László; Karsaï, I.; Vida, Gyula; Láng, L.; Bedö, Z.

doi:10.1007/978-94-017-3674-9_21

Cited by 8 publications

(8 citation statements)

References 2 publications

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“…Similar to subunit 5 encoded on chromosome 1D, 2* B contains five cysteine residues (Juhµsz et al 2001), in contrast with the x-type HMWGSs which generally contain four cysteine residues. However, there is an important difference between the two subunits in the localization of the extra cysteine.…”

Section: Resultsmentioning

confidence: 99%

“…The allele, designated as Glu-A1x2* B , was identified by molecular markers and is a mutant variant of the known 1Ax2* gene (Juhµsz et al 2001) (Fig. 2).…”

Section: Resultsmentioning

confidence: 99%

“…Since the sequence was 100% similar to that of the known 1Ax2* gene, another primer pair was designed to determine the sequence overlapping the 3 0 end of the 1,289-bp fragment. The new PCR product -300 bp in size -was cloned and the nucleotide sequence was determined (Juhµsz et al 2001). The entire identified mutant gene, 1Ax2* B was amplified using a primer pair specific to 1Ax-type genes, published by D' Ovidio et al (1995).…”

Section: Storage Protein Compositionmentioning

confidence: 99%

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Bánkúti 1201—an old Hungarian wheat variety with special storage protein composition

et al. 2003

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Bánkúti 1201, an old Hungarian wheat variety with special quality traits, was analysed to determine the relationships between its storage protein composition and superior quality-attributes for breadmaking. Based on the storage protein composition, the variety appears to have the nature of a population, containing several genotypes with different gluten protein alleles. Using molecular markers, a new mutant x-type HMW glutenin allele was identified, containing an extra cysteine residue and showing a moderate, positive-effect on gluten properties. In lines possessing subunits Bx7+By8 the overexpression of the Bx-type subunit could be detected, resulting in a higher unextractable polymeric protein (UPP) content and increased dough strength. It was found that the presence or absence of subunit Bx7 has an equilibrating effect on the dough extensibility, which is generally characteristic of the Bánkúti 1201 population. The complex good bread-making quality of the variety, which has strong but highly extensible dough, is probably due to the balance between lines which express subunit Bx7 and those which do not.

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Section: Resultsmentioning

confidence: 99%

“…The allele, designated as Glu-A1x2* B , was identified by molecular markers and is a mutant variant of the known 1Ax2* gene (Juhµsz et al 2001) (Fig. 2).…”

Section: Resultsmentioning

confidence: 99%

Section: Storage Protein Compositionmentioning

confidence: 99%

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Bánkúti 1201—an old Hungarian wheat variety with special storage protein composition

et al. 2003

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“…Genetic erosion is a process linked with modern agriculture and implies that the normal addition and disappearance of genetic variability in a population is altered so that net change in diversity is negative (Gregová et al, 1997). Using electrophoretic analyses of wheat glutenins it is sometimes possible to detect new HMW -GS alleles also in landraces (van Hintum and Ellings, 1991;Tahir et al, 1996, Gregová et al, 1999Juhász et al, 2001, Gregová et al, 2006. One hundred and eight hexaploid wheat accessions originating from Slovakia (32 cultivars), Czech Republic (15), Hungary (14), Germany (18) and France (29) were evaluated for high molecular weight glutenin subunits using SDS -PAGE.…”

Section: Resultsmentioning

confidence: 99%

Genetic Diversity of Glu-1 in European Wheat Genetic Resources and Varieties

Hlozáková¹,

Gregová²,

Gálová³

2015

J microb biotech food sci

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“…Buonocore et al [10] suggested that this “extra” cysteine residue might be the major factor explaining why this gluten subunit is associated with good quality. In the 1Ax2* B subunit, an x-type HMW-GS encoded at the Glu-A1 locus, there is a cysteine residue in the central domain in a different position compared to that in 1Dx5 [12]. …”

Section: Introductionmentioning

confidence: 99%

Proteogenomic Characterization of Novel x-Type High Molecular Weight Glutenin Subunit 1Ax1.1

Ribeiro

Bancel

Faye

et al. 2013

IJMS

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Analysis of Portuguese wheat (Triticum aestivum L.) landrace ‘Barbela’ revealed the existence of a new x-type high molecular weight-glutenin subunit (HMW-GS) encoded at the Glu-A1 locus, which we named 1Ax1.1. Using one-dimensional and two-dimensional electrophoresis and mass spectrometry, we compared subunit 1Ax1.1 with other subunits encoded at the Glu-A1 locus. Subunit 1Ax1.1 has a theoretical molecular weight of 93,648 Da (or 91,508 Da for the mature protein) and an isoelectric point (pI) of about 5.7, making it the largest and most acidic HMW-GS known to be encoded at Glu-A1. Specific primers were designed to amplify and sequence 2601 bp of the Glu-A1 locus from the ‘Barbela 28’ wheat genome. A very high level of identity was found between the sequence encoding 1Ax1.1 and those encoding other alleles of the locus. The major difference found was an insertion of 36 amino acids in the central repetitive domain.

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Identification, Cloning and Characterisation of a HMW-Glutenin Gene from an Old Hungarian Wheat Variety, Bánkúti 1201

Cited by 8 publications

References 2 publications

Bánkúti 1201—an old Hungarian wheat variety with special storage protein composition

Bánkúti 1201—an old Hungarian wheat variety with special storage protein composition

Genetic Diversity of Glu-1 in European Wheat Genetic Resources and Varieties

Proteogenomic Characterization of Novel x-Type High Molecular Weight Glutenin Subunit 1Ax1.1

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