Post-translational cleavage of HMW-GS Dy10 allele improves the cookie-making quality in common wheat (Triticum aestivum).

ABSTRACT: 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 decre

SUBMITTER: Wang Y 

PROVIDER: S-EPMC10236088 | biostudies-literature | 2021 Aug

REPOSITORIES: biostudies-literature