Isolation and Functionality Testing of Low Molecular Weight Glutenin Subunits

Sissons, Mike; Békés, F.; Skerritt, John H.

doi:10.1094/cchem.1998.75.1.30

Cited by 45 publications

(18 citation statements)

References 13 publications

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“…The role of HMW glutenins in wheat quality, particularly dough strength, is well established (Payne et al 1979;Payne 1987;Shewry et al 1992). LMW glutenins also have significant effects on wheat quality through both additive and epistatic interactions, particularly with HMW glutenins (Damidaux et al 1978;Gupta et al 1989Gupta and MacRitchie 1994;Nieto-Taladriz et al 1994;SontogStrohm et al 1996;Sissons et al 1998;Luo et al 2001;Eagles et al 2002;Tranquilli et al 2002). However, the exact role or contribution of individual LMW glutenin subunits or their alleles to wheat quality is not fully understood.…”

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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Section: Introductionmentioning

confidence: 99%

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

et al. 2004

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“…LMW glutenins comprise about 40% of the total endosperm proteins and 60-70% of glutenins. As the major components of wheat storage proteins, LMW-GS fractions have been found to be significantly correlated with dough extensibility (Gupta et al 1989;Metakovsky et al 1990), dough-mixing time (Sissons et al 1998) and dough strength (Tanaka et al 2005). In the past several decades, however, there have been fewer structure and function studies of LMW-GSs compared with HMW-GSs because of the similar mobilities of a large number of subunits in SDS-PAGE analysis and the difficulty of separation and characterization.…”

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confidence: 99%

Characterization and comparative analysis of three low molecular weight glutenin C-subunit genes isolated from Aegilops tauschii

Pei¹,

Wang²,

An³

et al. 2007

Can. J. Plant Sci.

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-M. 2007. Characterization and comparative analysis of three low molecular weight glutenin C-subunit genes isolated from Aegilops tauschii. Can. J. Plant Sci. 87: 273-280. Three low molecular weight glutenin subunit (LMW-GS) genes from T121, T128 and T132 accessions of Aegilops tauschii (DD, 2n = 2x = 14) were amplified using allelic-specific PCR primers. The amplified products with a size of about 900 bp were cloned and sequenced. Three complete coding sequences of LMW-GS with 918 bp, 921 bp and 918 bp were obtained and named as LMW-T121, LMW-T128, LMW-T132, respectively. Each gene contained a complete open reading frame and had no introns. The deduced amino acid sequences showed that all belonged to LMW-m type subunit with a predicted molecular weight of about 32 kDa, corresponding to the size of LMW C-subunits. All three subunits possessed eight cysteine residues and had greater homology with previously characterized LMW-m subunits from bread wheat and related species than LMW-s or LMW-i sequences. Some amino acid substitutions and insertion/deletion variations among the sequences were detected. The corresponding three C-subunits in seed endosperm encoded by LMW-T121, LMW-T128, LMW-T132, respectively, were identified and confirmed by SDS-PAGE, MALDI-TOF-MS and direct N-terminal amino acid sequencing. Phylogenetic analysis demonstrated that LMW-m and LMW-s type subunit genes possessed higher identity and they were obviously separated from LMW-i type subunit genes. The LMW-m type might be the primitive form while the LMW-s and LMW-i types are variant forms.

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“…1). These 16 lines GS polypeptides incorporated into the flour have are identical to Chinese Spring for all chromosome a dough strengthening effect 18 . These results, topairs except 1A, reducing genetic variation among gether with correlation studies of LM r -GS allelic lines and increasing the sensitivity of the exvariation and dough properties 9,19 , suggest that periments to detect small effects of loci located on differences in dough strength are mainly originated chromosome 1A on CMQ and predictive tests for in the LM r -GS rather than in the linked gliadin BMQ.…”

Section: Introductionmentioning

confidence: 95%

“…However, all previous Spring 31 and QTL analysis showed that Cheyenne studies aimed to differentiate the effect of these allele 2 * was associated with a 19% increase in SDS two linked loci have shown that the allelic variation sedimentation volume 46 compared to the 13·6% at the LM r -GS is the responsible for the observed increase observed here for the T. monococcum allele. effects on gluten strength 9,[16][17][18][19] . This result suggests that the beneficial effect of the T. monococcum allele will not be superior to that of the active T. aestivum 2 * allele.…”

Section: Loci No Rsls Were Available With Recombinationmentioning

confidence: 99%

Effect of Triticum monococcum glutenin loci on cookie making quality and on predictive tests for bread making quality

Tranquilli

Cuniberti

Gianibelli

et al. 2002

Journal of Cereal Science

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The effects of Triticum monococcum glutenin loci on cookie making quality and predictive tests for bread making quality were evaluated in recombinant substitution lines (RSLs) between chromosome 1A m from T. monococcum and chromosome 1A from Chinese Spring. All four combinations of high molecular weight (HM r -GS) and low molecular weight glutenin alleles (LM r -GS) were studied in a factorial design to evaluate their interactions. Grain protein content was used as a covariable to evaluate the effect of these loci independently of the variation in protein content among lines. No significant interactions were detected indicating an additive effect. RSLs carrying the HM r -GS from T. monococcum showed a 13·6% increase in SDS sedimentation volume (p=0·004) and a significant reduction in cookie diameter (−5·2%, p=0·02), and cookie quality (−6·8%, p=0·02). RSLs carrying the LM r -GS from T. monococcum showed a significant decrease in the proportion of polymeric protein (−2·8%, p<0·0001), SDS sedimentation volume (−8·1%, p=0·03) and gluten strength (−16·5%, p=0·01), and a significant increase in cookie quality (5·9%, p=0·05). The T. monococcum LM r -GS allele has potential value to be used in soft wheat breeding programs. These results suggest that diploid T. monococcum could be a valuable source for new allelic variation for storage proteins loci and new quality characteristics.

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Isolation and Functionality Testing of Low Molecular Weight Glutenin Subunits

Cited by 45 publications

References 13 publications

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

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

Characterization and comparative analysis of three low molecular weight glutenin C-subunit genes isolated from Aegilops tauschii

Effect of Triticum monococcum glutenin loci on cookie making quality and on predictive tests for bread making quality

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