Fig 1.
Identification of lysine acetylation proteins in Solenopsis invicta.
(A) Mass error distribution of all identified peptides. (B) Distribution of acetylated peptide length.
Fig 2.
Identification of lysine acetylation sites in Solenopsis invicta.
(A) Basic statistical figure for MS results. (B) Numbers of acetylated sites per protein. (C) Motif enrichment heat map of upstream and downstream amino acids for all identified Kac sites. Red indicates amino acids that are significantly enriched near the Kac site, and green indicates amino acids that are significantly reduced near the Kac site.
Fig 3.
Gene Ontology (GO) classification and subcellular location prediction of lysine acetylation proteins in Solenopsis invicta.
The GO categories indicated biological process, cellular component, and molecular function. (A) GO classification based on biological process. (B) GO classification based on cellular component. (C) GO classification based on molecular function. (D) Subcellular localization of proteins corresponding to Kac sites. (E) Kac sites of venom allergen Sol i 2, Sol i 3, and Sol i 4 located in the extracellular.
Fig 4.
Gene Ontology (GO) and domain enrichment of proteins corresponding to lysine acetylation sites in Solenopsis invicta.
(A) GO enrichment bubble plot of proteins in biological processes. (B) GO enrichment bubble plot of proteins in cellular components. (C) GO enrichment bubble plot of proteins in molecular functions. (D) Protein domain enrichment bubble plot of proteins.
Fig 5.
Bubble plot of KEGG pathway enrichment of proteins corresponding to lysine acetylation sites in Solenopsis invicta.
Fig 6.
Significantly enriched KEGG pathway in phagosome of Solenopsis invicta.
Lysine acetylation proteins are marked in red.
Fig 7.
Significantly enriched KEGG pathway in arginine and proline metabolism of Solenopsis invicta.
Lysine acetylation proteins are marked in red.
Fig 8.
V-type proton ATPase subunit G and tubulin alpha chain in Solenopsis invicta were conserved among various ant species.
The red star denotes the conserved lysine residues, and these results were analyzed by DNASTAR software. (A) V-type proton ATPase subunit G. (B) Tubulin alpha chain. (C) arginine kinase.
Fig 9.
Protein–Protein Interaction (PPI) networks of proteins corresponding to lysine acetylation sites in Solenopsis invicta.
(A) PPI network related to ribosome. (B) PPI network related to oxidative phosphorylation. (C) PPI network related to aminoacyl-tRNA biosynthesis. (D) PPI network related to proteasome. (E) PPI network related to carbon metabolism. (F) PPI network related to metabolic pathways.
Fig 10.
Overviews of lysine acetylation (Kac) proteins in Solenopsis invicta.
(A) An overview of Kac by SDS-PAGE analysis. (B) An overview of Kac by Western blot analysis. 20 μg protein/lane; Primary antibody: Anti-acetyllysine Antibody (PTM-101: 22838591 HB 14; 1:1000 dilution); 2nd antibody: Thermo, Pierce, Goat anti-Mouse IgG, (H+L), Peroxidase Conjugated, 31430, 1: 5000 dilution.