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Abstract
Crossing, backcrossing, and molecular marker-assisted background selection produced a soybean (Glycine max) near-isogenic line (cgy-2-NIL) containing the cgy-2 allele, which is responsible for the absence of the allergenic α-subunit of β-conglycinin. To identify α-null-related transcriptional changes, the gene expressions of cgy-2-NIL and its recurrent parent DN47 were compared using Illumina high-throughput RNA-sequencing of samples at 25, 35, 50, and 55 days after flowering (DAF). Seeds at 18 DAF served as the control. Comparison of the transcript profiles identified 3,543 differentially expressed genes (DEGs) between the two genotypes, with 2,193 genes downregulated and 1,350 genes upregulated. The largest numbers of DEGs were identified at 55 DAF. The DEGs identified at 25 DAF represented a unique pattern of GO category distributions. KEGG pathway analyses identified 541 altered metabolic pathways in cgy-2-NIL. At 18DAF, 12 DEGs were involved in arginine and proline metabolism. The cgy-2 allele in the homozygous form modified the expression of several Cupin allergen genes. The cgy-2 allele is an alteration of a functional allele that is closely related to soybean protein amino acid quality, and is useful for hypoallergenic soybean breeding programs that aim to improve seed protein quality.
Highlights
Soy-seed-derived products and their nutritional quality are affected by the subunit composition of seed storage proteins [1,2,3,4]
We have examined the effect of cgy-2 allele on the amino acid composition and gene expression
Near-isogenic line (NIL) cgy-2-NIL, carrying the cyg-2 allele (Fig 1), used for this study were derived from an α-subunit-null population, which has previously been used by our group to develop α-subunit-null improved lines with a Chinese soybean genetic background [12]
Summary
Soy-seed-derived products and their nutritional quality are affected by the subunit composition of seed storage proteins [1,2,3,4]. Glycinin (11S globulin) and β-conglycinin (7S) are the two main proteins in soybean seeds, accounting for ~70% of total seed proteins. By manipulating the identified variant alleles of glycinin and β-conglycinin, it is possible to breed soybean varieties with modified protein compositions, ranging from extremely high to extremely low 11S:7S ratios, which have led to improved nutritional values and food-processing properties [1,5,6]. In the past three decades, efforts to develop 7S-low-type soybean lines have led to the availability of various 7S or 11S globulin protein subunit null varieties among soybean germplasms [1,7,8,9,10,11,12]. Β-conglycinin allergen-subunit-deficiency mutants have high nutritional value and low allergenic risk [1,5,6,13,14]
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