Proteome-Wide Analysis of Protein Disorder in Durum Wheat

Abstract

Introduction: Intrinsically Disordered Proteins (IDPs) are natively unstructured proteins. Interestingly, IDPs are ubiquitous and play key roles in cellular and proteins functions. While IDPs are studied in some proteomes, many remain to be uncovered Methods: The data were retrieved from MobiDB database version 4. Intrinsic disorder predictions are made with various prediction tools. We focus on IUpred-L predictions. Results: Here, we have explored the first large-scale study of IDPs in T. turgidum. Additionally, a comparative analysis of T. turgidum and T. aestivum IDPs was performed for highlighting the dis-order use in each species. The data indicated that the T.turgidum proteome is significantly more dis-ordered than the T. aestivum proteome. Gene ontology analysis revealed that IDPs in T. turgidum are mainly catalytic and binding proteins involved in regulation of cellular and metabolic processes. Conclusion: These findings may constitute a starting point for deeper understanding of IDP roles in stress tolerance and the mechanisms underlying the adaptation capacities differences between T. turgidium and related species.