https://doi.org/10.1007/s11032-021-01238-9
Yan Wang · Qing Chen · Yang Li · Zhenru Guo · Caihong Liu · Yongfang Wan · Malcolm Hawkesford · Jing Zhu · Wang Wu · Meiqiao Wei · Kan Zhao · Yunfeng Jiang · Yazhou Zhang · Qiang Xu · Li Kong · Zhien Pu · Mei Deng · Qiantao Jiang · Xiujin Lan · Jirui Wang · Guoyue Chen · Jian Ma · Youliang Zheng · Yuming Wei · Pengfei Qi
Abstract
Wheat is a major staple food crop world wide because of the unique properties of wheat four. High molecular weight glutenin subunits (HMW GSs), which are among the most critical determinants of wheat four quality, are responsible for the forma tion of glutenin polymeric structures via interchain disulfde bonds. We herein describe the identifcation 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-trans lational 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 inter chain disulfde bonds. Consequently, Dy10-m619SN expression decreased the size of glutenin polymers and weakened glutens, which resulted in wheat dough with improved cookie-making quality, with out changes to the glutenin-to-gliadin ratio. In this study, we clarifed the post-translational processing of HMW-GSs and revealed a new genetic resource use ful for wheat breeding.
Keywords
HMW-GS · Amino acid substitution · Polymer size · Wheat processing quality
