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Abstract: In the field, developing cereal grains are often exposed to short periods of very high temperature (>35 °C) that may dramatically affect grain yield and flour quality. Here we report on the effect of 4 h of heat shock (HS) at 38 °C applied on four consecutive days during the linear phase of storage compound accumulation on grain proteome of the winter bread wheat. At maturity the average single grain dry mass and the total quantity of nitrogen per grain were 25% and 16%, respectively lower for the HS treatment than for the control, resulting in a higher (+1.6% dm) grain protein concentration in HS grains. Individual albumin–globulin, gliadin and glutenin protein fractions from grains collected just before the HS and 1, 8, and 26 (ripeness maturity) days after the HS were quantified then analysed by 2-dimensional electrophoresis followed by MALDI-TOF and MS/MS identification. The quantity per grain of 10 gliadins and 3 low molecular weight glutenin subunit proteins were significantly affected by HS. Thirty-eight HS responsive albumin and globulin proteins were identified, including several enzymes involved in carbohydrate, redox, and lipid metabolisms. One protein was transitorily induced in response to HS. Detailed discussion of the expression of these proteins is presented. [Copyright &y& Elsevier]

Abstract: In bread wheat (Triticum aestivum L.), waxy genes are present at three loci (Wx-A1, Wx-B1 and Wx-D1) and are responsible for amylose synthesis in the grain. Near isogenic lines (NILs) of the agronomic cultivar Tremie with either one, two or three waxy null alleles were used to study the genome response to these null alleles through proteomic analysis of starch granule associated proteins of mature grain. Among the 352 spots that were revealed, 86 varied significantly between NILs. The main differences were observed for the granule bound starch synthase (GBSS), product of the waxy genes. A strong relation (R2 = 0.94) between the amount of GBSS per gram of starch granule and the amylose quantity in the grain was revealed through quantification of the GBSS in each NIL. The analysis of GBSS quantity for each NIL invalidated the additive hypothesis for the expression of this enzyme in (Wx-A1a Wx-D1a Wx-B1b) (Wx-D1a Wx-B1a Wx-A1b) and the normal form of Tremie. In addition, four proteins identified as inactive GBSS were increased (+144.9%) in the triple null isogenic form compared to the normal form of Tremie. The quantitative variations of the proteins present in starch granules support the idea of regulatory mechanisms between genomes. [ABSTRACT FROM AUTHOR]

Abstract: To investigate the impact of the 1BL.1RS translocation on dough strength and to understand how 1BL.1RS genotypes may overcome the loss of Glu-B3 and Gli-B1, proteomic profiles of 16 doubled haploid (DH) lines of similar glutenin composition but of different strength, as measured by Chopin''s alveograph, were compared. The results showed that 32 spots, mainly prolamins, were differentially expressed and that five others were specific to high-strength DH lines. The identification and quantification of the prolamin fractions on the two-dimensional (2D) electrophoresis gels demonstrated that the high-molecular weight glutenin sub-unit (HMW-GS) were up-regulated by 25% in 1BL.1RS DH lines, even though the corresponding genes were not located on the missing 1BS chromosome. The γ-gliadins were also up-regulated (by 36%) in such lines to counterbalance, to some extent, the loss of LMW-GS of Glu-B3. The polymeric prolamin fractions also accumulated in high-tenacity lines and decreased in high-extensibility lines confirming the role of the inter-chain disulfide bonds in resistance to deformation. In contrast, the monomeric fraction of α-gliadin favored extensibility and decreased tenacity by increasing the accumulation (+12%) of α-gliadins in high-extensibility lines; the Gli-A1 allele of the parent Toronit was found to be more abundant when compared to the Gli-A1 allele of parent 211.12014. [Copyright &y& Elsevier]

Wheat grain storage proteins, i.e. the gluten proteins, and alpha-amylase trypsin inhibitors are partially resistant to gastrointestinal digestion. They figure among the wheat components that are potential triggers of non-celiac wheat sensitivity. To explore the digestibility of bread wheat proteins in relation to heritable plant traits, old and modern wheat varieties grown in two environments were genotyped, phenotyped, and processed into breads, which were partially digested in vitro in a system resembling human digestion. The extent of proteolysis measured after 2 h of digestion was variable. Digestion of proteins present in bread made from old wheat cultivars registered before 1960 and modern cultivars registered after 1960 was similar. No major plant trait was correlated to partial protein digestibility of bread from cultivars with high grain protein content. The protein digestibility of bread from high yield cultivars was influenced by protein composition, as well as the genetic distance per chromosome from a reference variety. Improving high yield cultivars by breeding for highly digestible proteins might help to mitigate adverse reactions to a range of wheat proteins in susceptible individuals. [Display omitted] • Breads made from distinct wheat flours are not digested at the same degree in vitro. • Old and modern cultivars do not differ in bread in vitro protein digestibility. • Plant traits of high yield cultivars are linked to partial protein digestibility. [ABSTRACT FROM AUTHOR]

Abstract: Starch is composed of two types of glucose polymers: amylose and amylopectin. The Waxy (Wx) locus controls amylose synthesis in the wheat kernel. Hexaploid wheat has three Wx loci located on chromosomes 7A (Wx-A1), 4A (Wx-B1), and 7D (Wx-D1). Eight near isogenic lines (NILs) of Triticum aestivum cv. Tremie with one, two or three Wx null alleles were used. The albumin–globulin fraction, and amphiphilic proteins were separated using 2-dimensional electrophoresis (2DE) allowing the changes in the waxy kernel to be identified. Albumin–globulin fraction showed overexpression of sucrose synthases in the waxy NILs compared to the normal form of Tremie and a decrease in many proteins related to stress and defence metabolism such as serpins. A subunit of ADP-glucose pyrophosphorylase (AGPase), which is known to play a major role in starch synthesis, was also shown to be down regulated in the waxy NILs. Amphiphilic proteins confirmed the observations made on the albumin–globulin fraction with a decrease in a stress-related protein. These different regulations linked to observations made on wheat kernel (thousand kernel weight (TKW), protein amount per grain, size and distribution of the starch granules) led to formulation of the hypothesis that waxy endosperm does not reach maturity of the wild-type endosperm. [Copyright &y& Elsevier]