Abstract
A wheat cultivar “Chinese Spring” chromosome substitution line CS-1Sl(1B), in which the 1B chromosome was substituted by 1Sl from Aegilops longissima, was developed and found to possess superior dough and breadmaking quality. The molecular mechanism of its super quality conformation is studied in the aspects of high molecular glutenin genes, protein accumulation patterns, glutenin polymeric proteins, protein bodies, starch granules, and protein disulfide isomerase (PDI) and PDI-like protein expressions. Results showed that the introduced HMW-GS 1Sl×2.3* and 1Sly16* in the substitution line possesses long repetitive domain, making both be larger than any known x- and y-type subunits from B genome. The introduced subunit genes were also found to have a higher level of mRNA expressions during grain development, resulting in more HMW-GS accumulation in the mature grains. A higher abundance of PDI and PDI-like proteins was observed which possess a known function of assisting disulfide bond formation. Larger HMW-GS deposited in protein bodies were also found in the substitution line. The CS substitution line is expected to be highly valuable in wheat quality improvement since the novel HMW-GS are located on chromosome 1Sl, making it possible to combine with the known superior D×5+Dy10 subunits encoded by Glu-D1 for developing high quality bread wheat.
Highlights
Wheat (Triticum aestivum L.) is one of the three most important grain crops in the world
HMW-GS only account for about 5–10% of the total proteins in mature seeds, approximately 67% of the variation of baking parameters among wheat cultivars can be attributed to differences in HMW-GS compositions [5,6,7,8]
The results showed that the 1Sl62.3* and 1Sly16* subunits were identified as HMWGS gi|47834185 (x-type HMW-GS from Aegilops bicornis) and gi|24474920 (y-type HMW-GS in T. aestivum), respectively (Table S2)
Summary
Wheat (Triticum aestivum L.) is one of the three most important grain crops in the world. Its flour and dough have unique physical properties for producing bread, cakes, biscuits, pasta and noodles. These unique properties are conferred by the mechanical properties of the gluten proteins mainly consisting of gliadins and glutenins. Gliadins are single chain molecules and impart dough extensibility while glutenins, including high and low molecular weight glutenin subunits (HMW-GS and LMW-GS), consist of protein subunits present in polymers stabilized by interchain disulphide bonds and give dough viscoelasticity [2,3]. According to previous studies [2,3,4], the HMW-GS confers dough strength while the LMW-GS is responsible for dough extensibility. HMW-GS only account for about 5–10% of the total proteins in mature seeds, approximately 67% of the variation of baking parameters among wheat cultivars can be attributed to differences in HMW-GS compositions [5,6,7,8]
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