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Characterization of a novel variant HMW‐glutenin gene from Elymus canadensis
Qian‐Tao Jiang,Yu‐Ming Wei,Tao Liu,Ji‐Rui Wang,Zhi‐En Pu,Xiu‐Jin Lan,You‐Liang Zheng,Zhen‐Xiang Lu 한국유전학회 2010 Genes & Genomics Vol.32 No.4
High molecular weight (HMW) glutenin subunits (GS) play a key role in the determination of end‐use quality of wheat and other cereal crops. In this study, we report the isolation and characterization of both promoter region and ORF of novel HMW‐GS allele 1St1.3 from a perennial Triticeae species,Elymus canadensis. The amino acid (AA) sequences of E. canadensis 1St1.3 were deduced as 434 aa. Its protein primary structure comprises a signal peptide with a conserved N‐terminal domain, a central repetitive domain and a C‐terminal domain. E. canadensis 1St 1.3 possesses several distinct characteristics which are different from those of wheat HMW‐GSs. The N‐terminal domains of E. canadensis 1St 1.3 resemble that of y‐type subunits, while their C‐terminal domains are more similar to x‐type subunits. The deletion of 85 bp fragment has been observed in promoter region of 1St 1.3, however which has not interrupted the expression of this gene. Our results indicate that 1St 1.3 is novel HMW‐GS variants which will be valuable for enhancing our understanding of structural differentiation and the evolutionary relationship among HMW‐GSs in Triticeae species.
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Adaptive polymorphism of tetrameric alpha-amylase inhibitors in wild emmer wheat
Ji-Rui Wang,Mei Deng,Ya-Xi Liu,Xin Qiao,Zhen-Hong Chen,Qian-Tao Jiang,Zhi-En Pu,Yu-Ming Wei,Eviatar Nevo,You-Liang Zheng 한국유전학회 2011 Genes & Genomics Vol.33 No.4
α-Amylase inhibitors are attractive candidates for the control of seed weevils as these insects are highly dependent on starch as an energy source. Wheat tetrameric α-amylase inhibitor (WTAI) is a mixture (60 kDa) of 3 units: WTAI-CM2 plus 2 WTAI-CM3 plus WTAI-CM16, where none of the subunits is active on its own. A total of 334 gene sequences were obtained from 14 populations (131 accessions= genotypes) of wild emmer wheat. The frequencies of SNPs in WTAI-CM2,WTAI-CM3 and WTAI-CM16 were 1 out of 87.6, 101.4, and 108.0 bases, where 5, 5 and 4 SNPs were detected in the coding sequence, respectively. The nucleotide sequence of each unit of tetrameric α-amylase inhibitors were much more conserved than that of dimeric or monomeric inhibitors. The wild emmer wheat populations showed diversity on three WTAI loci,both between and within populations. It was revealed that WTAI were naturally selected for across populations by a ratio of dN/dS as expected. The results of purifying and positive selection hypothesis (p<0.05) also showed that the sequences of WTAI were contributed by natural selection, which ensures the protein function conservation as well as the inhibition diversity with insects amylase enzyme. Ecological factors, singly or in combination, explained a significant proportion of the variations in the SNPs. Ecological factors have an important evolutionary role in gene differentiation at these loci, and tetrameric α-amylase inhibitors are obviously adaptively selected under different environments.
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