scholarly journals Development of reduced gluten wheat enabled by determination of the genetic basis of thelys3alow hordein barley mutant

2018 ◽  
Author(s):  
Charles P. Moehs ◽  
William J. Austill ◽  
Aaron Holm ◽  
Tao A. G. Large ◽  
Dayna Loeffler ◽  
...  
Keyword(s):  
Celiac Disease ◽  
Storage Proteins ◽  
Single Gene ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Nucleotide Polymorphisms ◽  
Related Condition ◽  
Single Nucleotide ◽  
Wheat Gene

AbstractCeliac disease is the most common food-induced enteropathy in humans with a prevalence of approximately 1% world-wide [1]. It is induced by digestion-resistant, proline- and glutamine-rich seed storage proteins, collectively referred to as “gluten,” found in wheat. Related prolamins are present in barley and rye. Both celiac disease and a related condition called non-celiac gluten sensitivity (NCGS) are increasing in incidence [2] [3]. This has prompted efforts to identify methods of lowering gluten in wheat, one of the most important cereal crops. Here we used BSR-seq (Bulked Segregant RNA-seq) and map-based cloning to identify the genetic lesion underlying a recessive, low prolamin mutation (lys3a) in diploid barley. We confirmed the mutant identity by complementing thelys3amutant with a transgenic copy of the wild type barley gene and then used TILLING (Targeting Induced Local Lesions in Genomes) [4] to identify induced SNPs (Single Nucleotide Polymorphisms) in the three homoeologs of the corresponding wheat gene. Combining inactivating mutations in the three sub-genomes of hexaploid bread wheat in a single wheat line lowered gliadin and low molecular weight glutenin accumulation by 50-60% and increased free and protein-bound lysine by 33%. This is the first report of the combination of mutations in homoeologs of a single gene that reduces gluten in wheat.

Determination of Seed Storage Proteins and Total Isoflavones in Wild and Cultivated Soybeans

2009 ◽  
Vol 19 (1) ◽  
pp. 115-118
Author(s):  
Savithiry S. Natarajan ◽  
Devanand L. Luthria ◽  
Qijian Song ◽  
Perry Cregan
Keyword(s):  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins

scholarly journals Studying common wheat material from crosses with Aegilops biuncialis vis. using markers for chromosome 1U

2019 ◽  
Vol 25 ◽  
pp. 55-59
Author(s):  
N. A. Kozub ◽  
I. A. Sozinov ◽  
H. Ya. Bidnyk ◽  
N. A. Demianova ◽  
O. I. Sozinova ◽  
...  
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Common Wheat ◽  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Bread Making ◽  
Wheat Gene ◽  
The Common ◽  
Gli 1

Aim. The aim of the research was to study common wheat material developed from crosses with Aegilops biuncialis Vis. using storage protein loci as markers for chromosome 1U. Methods. SDS and APAG electrophoreses of seed storage proteins were employed to identify alleles at the Glu-1 and Gli-1 loci. The following markers of chromosome 1U of Ae. biuncialis were used: the Glu-U1 locus encoding high-molecular-weight glutenin subunits located on the long arm (1UL) and the gliadin locus Gli-U1 on the short arm (1US). Results. In F6–F7, elimination of chromosome 1U material with a frequency of about 0.222 proceeded. This indicates selection against unbalanced genotypes, which could be tracked using markers for chromosome 1U. In wheat F4–F6 hybrids from crosses with Ae. biuncialis, we revealed a high frequency of formation of genotypes possessing the 1UL arm and lacking 1US. Conclusions. Since the Glu-U1 locus on the arm 1UL encodes high-molecular-weight subunits which directly determine bread-making quality, the developed wheat material is a source of a new allele of this locus introgressed from Ae. biuncialis for enriching the common wheat gene pool. Keywords: Triticum aestivum, Aegilops biuncialis, storage proteins, introgression.

Evidence that the N-terminal extension of the Vicieae convicilin genes evolved by intragenic duplications and trinucleotide expansions

Genome ◽  
2001 ◽  
Vol 44 (6) ◽  
pp. 1022-1030 ◽  
Author(s):  
L E Sáenz de Miera ◽  
M Pérez de la Vega
Keyword(s):  
Amino Acids ◽  
Lens Culinaris ◽  
Storage Proteins ◽  
Phylogenetic Analyses ◽  
Single Gene ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Gene Families ◽  
Plant Seed ◽  
Vicilin Gene

This study was aimed to identify lentil (Lens culinaris subsp. culinaris) convicilin genes and to carry out a comparative analysis of these genes in the tribe Vicieae. Convicilins differ from vicilins, a related group of plant seed storage proteins, mainly by the presence of an additional sequence of amino acids in the sequence corresponding to the first exon, referred as the N-terminal extension. A single gene for convicilin, a component of legume seed storage proteins, was identified in the cultivated lentil. In this species, the N-terminal extension is formed by a stretch of 126 amino acids of which 59.2% are charged amino acids: 29.6% glutamic acid, 3.2% aspartic acid, 14.4% arginine, 8.8% lysine, and 3.2% histidine. This lentil convicilin sequence is similar to the sequence of convicilins in other species of the tribe Vicieae. However, the size of the N-terminal extension clearly differs among convicilins. Sequence comparison and phylogenetic analyses including convicilin and vicilin of Vicieae species indicated that the differentiation between vicilins and convicilins predated the differentiation of the two vicilin gene families (47- and 50-kDa vicilins), and that the N-terminal extension evolved mainly by a series of duplications of short internal sequences and triplet expansions, the predominant one being GAA.Key words: convicilin, evolution by duplications, Lens culinaris Medik., lentil, legumes, trinucleotide expansion.

Development of a simple method for the determination of single nucleotide polymorphisms

2010 ◽  
Vol 34 (8) ◽  
pp. S75-S75
Author(s):  
Weifeng Zhu ◽  
Zhuoqi Liu ◽  
Daya Luo ◽  
Xinyao Wu ◽  
Fusheng Wan
Keyword(s):  
Single Nucleotide Polymorphisms ◽  
Nucleotide Polymorphisms ◽  
Simple Method ◽  
Single Nucleotide

Milling Characteristics and Distribution of Seed Storage Proteins in Rice with Various Grain Shapes

2009 ◽  
Vol 35 (2) ◽  
pp. 317-323 ◽  
Author(s):  
Li-Hui ZHOU ◽  
Qiao-Quan LIU ◽  
Ming-Hong GU
Keyword(s):  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Milling Characteristics

scholarly journals Wheat (Triticum aestivum L.) TaHMW1D Transcript Variants Are Highly Expressed in Response to Heat Stress and in Grains Located in Distal Part of the Spike

Plants ◽  
2021 ◽  
Vol 10 (4) ◽  
pp. 687
Author(s):  
Chan Seop Ko ◽  
Jin-Baek Kim ◽  
Min Jeong Hong ◽  
Yong Weon Seo
Keyword(s):  
Heat Stress ◽  
High Temperature ◽  
Temperature Stress ◽  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Grain Filling ◽  
High Temperature Stress ◽  
Two Dimensional Gel Electrophoresis ◽  
Transcript Variants

High-temperature stress during the grain filling stage has a deleterious effect on grain yield and end-use quality. Plants undergo various transcriptional events of protein complexity as defensive responses to various stressors. The “Keumgang” wheat cultivar was subjected to high-temperature stress for 6 and 10 days beginning 9 days after anthesis, then two-dimensional gel electrophoresis (2DE) and peptide analyses were performed. Spots showing decreased contents in stressed plants were shown to have strong similarities with a high-molecular glutenin gene, TraesCS1D02G317301 (TaHMW1D). QRT-PCR results confirmed that TaHMW1D was expressed in its full form and in the form of four different transcript variants. These events always occurred between repetitive regions at specific deletion sites (5′-CAA (Glutamine) GG/TG (Glycine) or (Valine)-3′, 5′-GGG (Glycine) CAA (Glutamine) -3′) in an exonic region. Heat stress led to a significant increase in the expression of the transcript variants. This was most evident in the distal parts of the spike. Considering the importance of high-molecular weight glutenin subunits of seed storage proteins, stressed plants might choose shorter polypeptides while retaining glutenin function, thus maintaining the expression of glutenin motifs and conserved sites.

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