Absence of Dx2 at Glu-D1 Locus Weakens Gluten Quality Potentially Regulated by Expression of Nitrogen Metabolism Enzymes and Glutenin-Related Genes in Wheat

• Published in: International journal of molecular sciences Vol. 21; no. 4; p. 1383
• Main Authors: Song, Lijun, Li, Liqun, Zhao, Liye, Liu, Zhenzhen, Xie, Tingting, Li, Xuejun
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI 18.02.2020; MDPI AG
• Subjects: glutenin-related gene; high-molecular-weight glutenin subunit dx2; nitrogen metabolism enzyme; protein body; wheat gluten quality; glutenin-related gene; protein body; wheat gluten quality; nitrogen metabolism enzyme; high-molecular-weight glutenin subunit Dx2
• ISSN: 1422-0067; 1422-0067
• DOI: 10.3390/ijms21041383

Absence of high-molecular-weight glutenin subunit (HMW-GS) Dx2 weakens the gluten quality, but it is unclear how the absence of Dx2 has these effects. Thus, we investigated the gluten quality in terms of cytological, physicochemical, and transcriptional characteristics using two near-isogenic lines with Dx2 absent or present at locus. Cytological observations showed that absence of Dx2 delayed and decreased the accumulation of protein bodies (PBs), where fewer and smaller PBs formed in the endosperm. The activity and gene expression levels of nitrogen assimilation and proteolysis enzymes were lower in HMW-D1a without Dx2 than HMW-D1p with Dx2, and thus less amino acid was transported for protein synthesis in the grains. The expression pattern of genes encoding Glu-1Dx2+1Dy12 was similar to those of three transcription factors, where these genes were significantly down-regulated in HMW-D1a than HMW-D1p. Three genes involving with glutenin polymerization were also down-regulated in HMW-D1a. These results may explain the changes in the glutenin and glutenin macropolymer (GMP) levels during grain development. Therefore, we suggest that the lower nitrogen metabolism capacity and expression levels of glutenin synthesis-related genes in HMW-D1a accounted for the lower accumulation of glutenin, GMP, and PBs, thereby weakening the structural‒thermal properties of gluten.