Systematic Analysis of the Lysine Acetylome in Candida albicans.

Candida albicans (C. albicans) is a worldwide cause of fungal infectious diseases. As a general post-translational modification (PTM), lysine acetylation of proteins play an important regulatory role in almost every cell. In our research, we used a high-resolution proteomic technique (LC-MS/MS) to present the comprehensive analysis of the acetylome in C. albicans. In general, we detected 477 acetylated proteins among all 9038 proteins (5.28%) in C. albicans, which had 1073 specific acetylated sites. The bioinformatics analysis of the acetylome showed a significant role in the regulation of metabolism. To be more precise, proteins involved in carbon metabolism and biosynthesis were the underlying objectives of acetylation. Besides, through the study of the acetylome, we found a universal rule in acetylated motifs: the +4, +5, or +6 position, which is an alkaline residue with a long side chain (K or R), and the +1 or +2 position, which is a residue with a long side chain (Y, H, W, or F). To the best of our knowledge, all screening acetylated histone sites of this study have not been previously reported. Moreover, protein-protein interaction network (PPI) study demonstrated that a variety of connections in glycolysis/gluconeogenesis, oxidative phosphorylation, and the ribosome were modulated by acetylation and phosphorylation, but the phosphorylated proteins in oxidative phosphorylation PPI network were not abundant, which indicated that acetylation may have a more significant effect than phosphorylation on oxidative phosphorylation. This is the first study of the acetylome in human pathogenic fungi, providing an important starting point for the in-depth discovery of the functional analysis of acetylated proteins in such fungal pathogens.