Involvement of sulfur assimilation in the low β subunit content of soybean seed storage protein revealed by comparative transcriptome analysis

The β subunit of soybean [Glycine max (L.) Merr.] seed storage protein is of great significance in sulfur-containing amino acid balance and soybean processing properties. The objective of this study was to elucidate the relationship between the β subunit and sulfur-containing amino acid composition, and the potential regulatory mechanism. The β subunit was independently accumulated in comparison with other major subunits (α/α′, acidic, basic, and A3) during seed filling, and a low level of β subunit content (BSC) was formed during the accumulation process. In low-BSC mature seeds, crude protein, oil content, and fatty acid composition were not changed, but sulfur-containing amino acids (Cys + Met) in the low-BSC seeds increased significantly (by 31.5%), suggesting that an internal regulatory mechanism within seed might be responsible for the rebalance of seed protein composition and that sulfur assimilation might be deeply involved in β subunit accumulation. Transcriptomic analysis revealed that genes involved in anabolism of cysteine, methionine, and glutathione were up-regulated but those involved in the catabolism of these compounds were down-regulated, suggesting a relationship between the elevation of methionine and glutathione and low BSC. Our study sheds light on seed composition in low BSC lines and on the potential molecular regulatory mechanism of β subunit accumulation, broadening our understanding of soybean seed protein synthesis and its regulation.