Abstract
Drought stress is becoming more prevalent with global warming, and has been shown to have large effects on gluten proteins linked to wheat bread making quality. Likewise, low temperature stress can detrimentally affect proteins in wheat. This study was done to determine the differential abundance of high molecular weight (HMW) glutenin proteins in a drought and low temperature stressed high quality hard red spring wheat cultivar (PAN3478), against a control. The treatments were applied in the greenhouse at the soft dough stage. HMW glutenin proteins were extracted from the flour, and were separated by using two-dimensional gel electrophoresis. Protein spots that had p values lower than 0.05 and fold values equal to or greater than 1.2 were considered to be significantly differentially abundant. These proteins were further analyzed by using tandem mass spectrometry. There was a 1.3 to 1.8 fold change in 17 protein spots due to the cold treatment. The drought treatment caused a 1.3 to 3.8 fold change in 19 protein spots. These spots matched either HMW or low molecular weight (LMW) glutenin subunits. In the latter case, the C subunits of LMW glutenins were notably found to be up-regulated under both stress conditions. All the proteins that have been identified can directly influence dough characteristics. Data are available via ProteomeXchange with the identifier PXD017578.
Highlights
In the last few years, there has been significant progress in protein separation and identification techniques, including two dimensional gel electrophoresis (2-DE), liquid chromatography, mass spectrometry (MS) and in the availability of databases and database searching [1]
The processing properties of wheat are largely determined by gluten proteins
The high molecular weight (HMW) glutenins are known to have a large effect on dough technological properties [22], and clearly proteins with peptide sequences that are similar, especially HMW glutenins DY12, PW212, PC256, HMW-glutenin subunits (GS) DX2 and
Summary
In the last few years, there has been significant progress in protein separation and identification techniques, including two dimensional gel electrophoresis (2-DE), liquid chromatography, mass spectrometry (MS) and in the availability of databases and database searching [1]. Among the most commonly used methods in proteomics, 2-DE allows easy resolution and visualization of thousands of protein species on a single gel, resolving proteoforms [2]. Proteomics can be used to understand how the genome regions are involved with grain protein composition, the involvement of enzymes and the expression of specific genes in different growing conditions [4,5]. In this way, proteomics in wheat are proving to be a powerful tool to elucidate the expression of proteins and how they contribute to the value of the grain.
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