Abstract
Posttranslational modifications (PTMs) of the whole proteome have become a hot topic in the research field of epigenetics, and an increasing number of PTM types have been identified and shown to play significant roles in different cellular processes. Protein lysine 2-hydroxyisobutyrylation (Khib) is a newly detected PTM, and the 2-hydroxyisobutyrylome has been identified in several species. Botrytis cinerea is recognized as one of the most destructive pathogens due to its broad host distribution and very large economic losses; thus the many aspects of its pathogenesis have been continuously studied. However, distribution and function of Khib in this phytopathogenic fungus are not clear. In this study, a proteome-wide analysis of Khib in B. cinerea was performed, and 5,398 Khib sites on 1,181 proteins were identified. Bioinformatics analysis showed that the 2-hydroxyisobutyrylome in B. cinerea contains both conserved proteins and novel proteins when compared with Khib proteins in other species. Functional classification, functional enrichment and protein interaction network analyses showed that Khib proteins are widely distributed in cellular compartments and involved in diverse cellular processes. Significantly, 37 proteins involved in different aspects of regulating the pathogenicity of B. cinerea were detected as Khib proteins. Our results provide a comprehensive view of the 2-hydroxyisobutyrylome and lay a foundation for further studying the regulatory mechanism of Khib in both B. cinerea and other plant pathogens.
Highlights
Protein posttranslational modifications (PTMs) are important regulatory mechanisms in all living cells and involved in almost all aspects of cellular processes
Our results show that Khib is an important Posttranslational modifications (PTMs) and is involved in the regulation of various cellular processes in the phytopathogenic fungus B. cinerea
To identify Khib sites in B. cinerea hyphae, affinity enrichment and high-resolution liquid chromatography–tandem mass spectrometry (LC-MS/MS) methods were used for proteomewide analysis following the standard workflow (Supplementary Figure 1A)
Summary
Protein posttranslational modifications (PTMs) are important regulatory mechanisms in all living cells and involved in almost all aspects of cellular processes. Multiple amino acid residues can be covalently modified by different groups (Macek et al, 2019). Protein acylation mainly occurs on lysine residues, which are modified by short-chain fatty acids donated by their corresponding acyl-coenzyme A (CoA) groups (Huang et al, 2018). The most studied protein acylation type is histone acetylation, which was discovered more than 50 years ago (Allfrey et al, 1964). Apart from acetyl groups, a variety of short-chain fatty acid groups have been discovered on lysine residues of mature proteins, including propionylation (Kpr), butyrylation (Kbu), crotonylation (Kcr), 2-hydroxyisobutyrylation (Khib), malonylation (Kmal), and succinylation (Ksu) (Walsh et al, 2005; Chen et al, 2007; Zhang et al, 2011; Huang et al, 2014; Zhao and Garcia, 2015)
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