Wheat is a major staple food crop worldwide because of the unique properties of wheat flour. High molecular weight glutenin subunits (HMW-GSs), which are among the most critical determinants of wheat flour quality, are responsible for the formation of glutenin polymeric structures via interchain disulfide bonds. We herein describe the identification of a new HMW-GS Dy10 allele (Dy10-m619SN). The amino acid substitution (serine-to-asparagine) encoded in this allele resulted in a partial post-translational cleavage that produced two new peptides. These new peptides disrupted the interactions among gluten proteins because of the associated changes to the number of available cysteine residues for interchain disulfide bonds. Consequently, Dy10-m619SN expression decreased the size of glutenin polymers and weakened glutens, which resulted in wheat dough with improved cookie-making quality, without changes to the glutenin-to-gliadin ratio. In this study, we clarified the post-translational processing of HMW-GSs and revealed a new genetic resource useful for wheat breeding.
Supplementary information: The online version contains supplementary material available at 10.1007/s11032-021-01238-9.
Keywords: Amino acid substitution; HMW-GS; Polymer size; Wheat processing quality.
© The Author(s), under exclusive licence to Springer Nature B.V. 2021.