Abstract
BackgroundsLysine 2-hydroxyisobutyrylation (Khib) is a newly discovered posttranslational modification (PTM) and has been identified in several prokaryotic and eukaryotic organisms. Fusarium graminearum, a major pathogen of Fusarium head blight (FHB) in cereal crops, can cause considerable yield loss and produce various mycotoxins that threaten human health. The application of chemical fungicides such as tebuconazole (TEC) remains the major method to control this pathogen. However, the distribution of Khib in F. graminearum and whether Khib is remodified in response to fungicide stress remain unknown.ResultsHere, we carried out a proteome-wide analysis of Khib in F. graminearum, identifying the reshaping of the lysine 2-hydroxyisobutyrylome by tebuconazole, using the most recently developed high-resolution LC–MS/MS technique in combination with high-specific affinity enrichment. Specifically, 3501 Khib sites on 1049 proteins were identified, and 1083 Khib sites on 556 modified proteins normalized to the total protein content were changed significantly after TEC treatment. Bioinformatics analysis showed that Khib proteins are involved in a wide range of biological processes and may be involved in virulence and deoxynivalenol (DON) production, as well as sterol biosynthesis, in F. graminearum.ConclusionsHere, we provided a wealth of resources for further study of the roles of Khib in the fungicide resistance of F. graminearum. The results enhanced our understanding of this PTM in filamentous ascomycete fungi and provided insight into the remodification of Khib sites during azole fungicide challenge in F. graminearum.
Highlights
Protein posttranslational modifications (PTMs), such as methylation, acetylation, and phosphorylation, play important roles in various biological events andZhao et al BMC Genomics (2022) 23:145 nonhistone proteins [1,2,3,4,5,6,7]
The results enhanced our understanding of this PTM in filamentous ascomycete fungi and provided insight into the remodification of Lysine 2-hydroxyisobutyrylation (Khib) sites during azole fungicide challenge in F. graminearum
The results showed that multiple protein bands larger than 25 kDa were detected in all the samples, indicating that Khib is widely distributed in F. graminearum
Summary
Protein posttranslational modifications (PTMs), such as methylation, acetylation, and phosphorylation, play important roles in various biological events andZhao et al BMC Genomics (2022) 23:145 nonhistone proteins [1,2,3,4,5,6,7]. Protein posttranslational modifications (PTMs), such as methylation, acetylation, and phosphorylation, play important roles in various biological events and. Khib can influence various biological processes, such as the regulation of gene expression, energy metabolism, protein translation, and secondary metabolism [1, 11,12,13]. Fusarium graminearum is the major causal agent of Fusarium head blight (FHB), a devastating disease of wheat and barley worldwide. The application of chemical agents such as tebuconazole (TEC) and carbendazim (BCM) remains the major method to control this disease. Extensive research on the mechanism of fungicide resistance in F. graminearum has been performed, but only a few studies on how PTMs participate in fungicide resistance have been reported
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