Abstract
BackgroundLysine acetylation in proteins is a ubiquitous and conserved post-translational modification, playing a critical regulatory role in almost every aspect of living cells. Although known for many years, its function remains elusive in Fusarium graminearum, one of the most important necrotrophic plant pathogens with huge economic impact.ResultsBy the combination of affinity enrichment and high-resolution LC-MS/MS analysis, large-scale lysine acetylome analysis was performed. In total, 577 lysine acetylation sites matched to 364 different proteins were identified. Bioinformatics analysis of the acetylome showed that the acetylated proteins are involved in a wide range of cellular functions and exhibit diverse subcellular localizations. Remarkably, 10 proteins involved in the virulence or DON (deoxynivalenol) biosynthesis were found to be acetylated, including 4 transcription factors, 4 protein kinases and 2 phosphatases. Protein-protein interaction network analysis revealed that acetylated protein complexes are involved in diversified interactions.ConclusionsThis work provides the first comprehensive survey of a possible lysine acetylome in F. graminearum and reveals previously unappreciated roles of lysine acetylation in the regulation of diverse biological processes. This work provides a resource for functional analysis of acetylated proteins in filamentous fungi.Electronic supplementary materialThe online version of this article (doi:10.1186/s12864-016-3361-3) contains supplementary material, which is available to authorized users.
Highlights
Lysine acetylation in proteins is a ubiquitous and conserved post-translational modification, playing a critical regulatory role in almost every aspect of living cells
Identification and analysis of lysine-acetylated proteins in F. graminearum Combination of immune-affinity purification and enrichment and high-resolution LC-mass spectrometry (MS)/MS proteomic method was employed to determine the acetylome of F. graminearum PH-1
The strategy and technologies used to analyze lysine acetylation in F. graminearum were the same to be used in P. sojae, and B. cinerea
Summary
Lysine acetylation in proteins is a ubiquitous and conserved post-translational modification, playing a critical regulatory role in almost every aspect of living cells. Acetylation of lysine residues in proteins is a dynamic and reversible post-translational modification (PTM) occurring ubiquitously in living cells in both prokaryotes and eukaryotes [1,2,3,4]. Lysine acetylation is catalyzed by lysine acetyltrasferases (KATs) and reversed by lysine deacetylases (KDACs) [5]. Through this reversible process the acetylation status of proteins is dynamically balanced for proper cellular regulation [6, 7]. Up to now, many non-histone proteins have been identified to be lysine acetylated as well. The wellcharacterized acetylated non-histone proteins mainly include metabolic enzymes, transcription factors, hormone receptors, signal transducers, chaperones and proteins of
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