Molecular cloning and characterization of five novel low molecular weight glutenin subunit genes from Tibetan wheat landraces (Triticum aestivum L.)

Lan, Qiuxia; Feng, Bo; Xu, Zhibin; Zhao, Guo-Jun; Wang, Tao

doi:10.1007/s10722-012-9877-8

Cited by 14 publications

(7 citation statements)

References 20 publications

(31 reference statements)

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“…The same number of cysteine residues was present in the LMW-m gene AY263369, which was probably associated with good properties of Chinese wheat cultivar Xiaoyan 6 (Zhao et al 2004). It has been suggested that the additional cysteine residue in LMW subunits might lead to a higher cross linkage with other glutenin subunits, which contributes to enhanced dough properties (Lan et al 2013). Comosa-M1 possessed seven cysteine residues, with the first cysteine residue replaced by tyrosine.…”

Section: Discussionmentioning

confidence: 99%

Characterization of novel LMW glutenin subunit genes at the Glu-M3 locus from Aegilops comosa

Huang

Jin

et al. 2018

3 Biotech

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We report the characterization of seven novel low-molecular-weight glutenin subunit (LMW-GS) genes from (2 = 2 = 14, MM). We found that all seven LMW-GS genes possessed the same primary structure shared by other known LMW-GSs. Three genes (, and ) encode LMW-m-type subunits, two ( and ) encode LWM-i-type subunits, and two ( and ) encode LWM-l-type subunits. The comosa-M1 possessed seven cysteine residues, which resulted from a single-nucleotide polymorphism (SNP) of the G-A transition in the fifth position of the N-terminal sequence. Two l-type subunits, comosa-L1 and comosa-L2, contained nine cysteine residues with an extra cysteine residue located in the signal peptide and repetitive domain. In addition, a long insertion of 13 residues (LGQQPQ8/LVQQPQ8) was present in the end of the C-terminal II. Phylogenetic analysis implied that the comosa-L2 may be the intermediate type during the evolution of LMW-l and LMW-i-type genes. Our results demonstrated that the novel LMW-GSs, such as comosa-M1, comosa-L1, and comosa-L2, may have positive effects on dough properties.

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Section: Discussionmentioning

confidence: 99%

Characterization of novel LMW glutenin subunit genes at the Glu-M3 locus from Aegilops comosa

Huang

Jin

et al. 2018

3 Biotech

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“…Ribeiro et al (2013) analyzed the Portuguese wheat landrace 'Barbela' and reported a new x-type HMW-GS encoded at the Glu-A1 locus that was named 1Ax1.1. Lan et al (2013) reported low-molecular weight glutenin subunits as the major components of glutenins, which were considered to be important for the end-use quality of wheat; however, Kaur et al (2013) reported the physico-chemical and rheological properties of Indian wheat cultivars varying in HMW-GS. Pompa et al (2013) reported that the gluten composition and expression influenced dough properties and were cultivar-and environment-dependent.…”

Section: Discussionmentioning

confidence: 99%

Genetic divergence for high-molecular weight glutenin subunits (HMW-GS) in indigenous landraces and commercial cultivars of bread wheat of Pakistan

Yasmeen¹,

Khurshid²,

Ghafoor³

2015

Genet. Mol. Res.

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ABSTRACT. Wheat flour quality is an important consideration in the breeding and development of new cultivars. A strong association between high-molecular weight glutenin subunits (HMW-GS) and bread making quality has resulted in the widespread utilization of HMW-GS in wheat breeding. In this study, we analyzed 242 lines of wheat, including landraces from the provinces of Punjab and Baluchistan, as well as the commercial varieties of Pakistan, to determine allelic variation in the Glu-A1, Glu-B1, and Glu-D1 loci encoding HMW-GS. Higher genetic diversity was observed for HMW-GS in landraces from Baluchistan, followed by landraces collected from Punjab and then commercial varieties. Rare and uncommon subunits were observed in Glu-B1, whereas Glu-A1 was less polymorphic. However, Glu-B1 was the highest contributor to overall diversity (78%), with a total of 31 rare alleles, followed by Glu-D1 (20%) with the high quality 5+10 allele and other variants. Commercial cultivars possessed favorable alleles, potentially from indirect selection for wheat flour quality by the breeders; however, this indirect selection 4830 F. Yasmeen et al. ©FUNPEC-RP www.funpecrp.com.br Genetics and Molecular Research 14 (2): 4829-4839 (2015) has decreased the pedigree base of commercial cultivars. The allelic combinations, including 2*, 5+10, and 17+18, showing high quality scores were frequent among landraces, indicating their usefulness in future crop improvement and breeding programs.

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“…However, in different papers, this terminology has already been applied ([22,23] just to cite the most recent ones).…”

Section: Discussionmentioning

confidence: 99%

An asparagine residue at the N-terminus affects the maturation process of low molecular weight glutenin subunits of wheat endosperm

et al. 2014

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BackgroundWheat glutenin polymers are made up of two main subunit types, the high- (HMW-GS) and low- (LMW-GS) molecular weight subunits. These latter are represented by heterogeneous proteins. The most common, based on the first amino acid of the mature sequence, are known as LMW-m and LMW-s types. The mature sequences differ as a consequence of three extra amino acids (MET-) at the N-terminus of LMW-m types. The nucleotide sequences of their encoding genes are, however, nearly identical, so that the relationship between gene and protein sequences is difficult to ascertain.It has been hypothesized that the presence of an asparagine residue in position 23 of the complete coding sequence for the LMW-s type might account for the observed three-residue shortened sequence, as a consequence of cleavage at the asparagine by an asparaginyl endopeptidase.ResultsWe performed site-directed mutagenesis of a LMW-s gene to replace asparagine at position 23 with threonine and thus convert it to a candidate LMW-m type gene. Similarly, a candidate LMW-m type gene was mutated at position 23 to replace threonine with asparagine. Next, we produced transgenic durum wheat (cultivar Svevo) lines by introducing the mutated versions of the LMW-m and LMW-s genes, along with the wild type counterpart of the LMW-m gene.Proteomic comparisons between the transgenic and null segregant plants enabled identification of transgenic proteins by mass spectrometry analyses and Edman N-terminal sequencing.ConclusionsOur results show that the formation of LMW-s type relies on the presence of an asparagine residue close to the N-terminus generated by signal peptide cleavage, and that LMW-GS can be quantitatively processed most likely by vacuolar asparaginyl endoproteases, suggesting that those accumulated in the vacuole are not sequestered into stable aggregates that would hinder the action of proteolytic enzymes. Rather, whatever is the mechanism of glutenin polymer transport to the vacuole, the proteins remain available for proteolytic processing, and can be converted to the mature form by the removal of a short N-terminal sequence.

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Molecular cloning and characterization of five novel low molecular weight glutenin subunit genes from Tibetan wheat landraces (Triticum aestivum L.)

Cited by 14 publications

References 20 publications

Characterization of novel LMW glutenin subunit genes at the Glu-M3 locus from Aegilops comosa

Characterization of novel LMW glutenin subunit genes at the Glu-M3 locus from Aegilops comosa

Genetic divergence for high-molecular weight glutenin subunits (HMW-GS) in indigenous landraces and commercial cultivars of bread wheat of Pakistan

An asparagine residue at the N-terminus affects the maturation process of low molecular weight glutenin subunits of wheat endosperm

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