Global analysis of lysine 2-hydroxyisobutyrylation during Fusarium graminearum infection in maize

Abstract

Proteins post-translational modification (PTMs) is necessary in the whole life process of organisms. Among them, lysine 2-hydroxyisobutyrylation (Khib) plays an important role in protein synthesis, transcriptional regulation, and cell metabolism. Khib is a newly identified PTM in several plant species. However, the function of Khib in maize was unclear. In this study, western blotting results showed that Khib modification level increased significantly after Fusarium graminearum infection, and 2,066 Khib modified sites on 728 proteins were identified in maize, among which 24 Khib sites occurred on core histones. Subcellular localization results showed that these Khib modified proteins were localized in cytoplasm, chloroplast, and nucleus. Then, comparative proteomic analysis of the defense response to F. graminearum infection showed that Khib modification participated in plant resistance to pathogen infection by regulating glycolysis, TCA cycle, protein synthesis, peroxisome, and secondary metabolic processes, such as benzoxazinoid biosynthesis, phenylpropanoid biosynthesis, jasmonic acid synthesis, and tyrosine and tryptophan biosynthesis. In addition, we also demonstrated that lysine 2-hydroxyisobutyrylation sites on histones were involved in the gene expression of pathogenesis-related proteins. Our results provide a new perspective for the study of plant disease resistance, and had directive significance of maize disease resistance for molecular breeding.

Histone 2-Hydroxyisobutyryltransferase Encoded by Afngg1 Is Involved in Pathogenicity and Aflatoxin Biosynthesis in Aspergillus flavus

“…As an important post-translational modification, 2-hydroxyisobutyrylation plays a vital role in protein synthesis, transcriptional regulation and metabolism [ 14 ]. In this study, we performed a functional analysis of histone 2-hydroxyisobutyryltransferase Afngg1 in A. flavus .…”

Functions of lysine 2‐hydroxyisobutyrylation and future perspectives on plants

“…In deacetylase inhibitor TSA (trichostatin A) [34]. These findings imply that HDACs were the key erasers of Khib in Arabidopsis, rice, and maize histones [36].…”

“…fungi bacteria [30], and plantae [15][16][17][31][32][33][34][35][36], such as Saccharomyces cerevisiae, Toxoplasma gondii, Escherichia coli, Proteus mirabilis, Candida albicans, Botrytis cinerea, Giardia lamblia, soybean, maize, rice, and wheat (Table 1). These studies showed that Khib sites are frequently conserved across diverse organisms, and Khib is a highly prevalent protein modification in many kinds of organisms.…”

“…Subsequently, the profiling of 2‐hydroxyisobutyrylome in different species was reported, which mainly lied on the efficient affinity enrichment at proteome‐wide with confirmed anti‐2‐hydroxyisobutyryllysine antibody conjugated agarose beads and LC–MS/MS analysis. Until now, thousands of Khib proteins have been identified in animal [12, 18, 20, 21], fungi [13, 22–29], fungi bacteria [30], and plantae [15–17, 31–36], such as Saccharomyces cerevisiae , Toxoplasma gondii , Escherichia coli , Proteus mirabilis , Candida albicans, Botrytis cinerea, Giardia lamblia, soybean , maize , rice, and wheat (Table 1). These studies showed that Khib sites are frequently conserved across diverse organisms, and Khib is a highly prevalent protein modification in many kinds of organisms.…”

Lysine 2‐Hydroxyisobutyrylation‐ and Succinylation‐Based Pathways Act Inside Chloroplasts to Modulate Plant Photosynthesis and Immunity

“…The histones H2A, H2B, H3.2 and H4 were modified even by 14 Khib sites (Figure 1d). We discovered more Khib sites and acylated proteins and a higher number of Khib sites per protein in cotton than those in citrus fruit, [22] Arabidopsis leaf, [23] maize stem, [24] and rice leaf and flower (Figure 1e). [25,26] To explore the subcellular distribution of Khib proteins, we performed a cellular compartment analysis of the Khib proteins.…”