Proteomic changes occuring in einkorn (Triticum monoccocum) grain during filling stages of development

Albumins and globulins of wheat endosperm represent about 20% of total grain proteins. Nutritionally, the albumins and globulins (non-glutens) have a very good amino acid balance. Many of these proteins are enzymes involved in metabolic activity. Most of these physiologically active proteins can also influence the processing and rheological properties of wheat flour.Incomplete knowledge of these enzymes and related proteins present in the endosperm of wheat limits our understanding of the biochemical events taking place in the grain during the first stages of its development. So it is necessary to study and evaluate qualitative and quantitative changes occurring during this process. To reach this objective, our study is based on Triticum monococcum (einkorn), a diploid wheat species, used as a model species of bread wheat (T. aestivum).We used a proteomic approach to identify the key actors during the filling stages of development in einkorn grain. Five stages were studied (200 to 600°Cd). Large-scale analysis using the gel free proteomic approach allowed us to identify a total of 2,475 proteins. Among these proteins, 512 (20.7%) were accurately quantified, 488 of them presented changes related to stage development, highlighting this dynamic process (Bonnot et al, 2017).Hierarchical cluster analysis revealed four major expression profiles throughout grain development. The classification of proteins identified by MS/MS in 17 different biochemical functions and nine molecular functions provided a picture of the temporal cellular processes involved. Several proteins differentially expressed and associated with grain development and/or quality were also shown.A co-accumulation network of all differentially expressed proteins mainly centred on enzymes involved in carbon and protein metabolism was finally established.