Abstract
Lysine acetylation of proteins, a major post-translational modification, plays a critical regulatory role in almost every aspects in both eukaryotes and prokaryotes. Yarrowia lipolytica, an oleaginous yeast, is considered as a model for bio-oil production due to its ability to accumulate a large amount of lipids. However, the function of lysine acetylation in this organism is elusive. Here, we performed a global acetylproteome analysis of Y. lipolytica ACA-DC 50109. In total, 3163 lysine acetylation sites were identified in 1428 proteins, which account for 22.1% of the total proteins in the cell. Fifteen conserved acetylation motifs were detected. The acetylated proteins participate in a wide variety of biological processes. Notably, a total of 65 enzymes involved in lipid biosynthesis were found to be acetylated. The acetylation sites are distributed in almost every type of conserved domains in the multi-enzymatic complexes of fatty acid synthetases. The provided dataset probably illuminates the crucial role of reversible acetylation in oleaginous microorganisms, and serves as an important resource for exploring the physiological role of lysine acetylation in eukaryotes.
Highlights
Post-translational modifications (PTMs) play an important role in modulating diverse cellular processes, which can change protein functions by introducing new functional groups such as phospho, acetyl, ubiquityl and methyl groups (Huang et al 2015; Santos et al 2011)
Proteome‐wide analysis of lysine acetylation sites and proteins in Y. lipolytica Yarrowia lipolytica ACA-DC 50109 was cultured in the oil production medium
To validate the MS data, the mass error of all the identified peptides were checked and the results showed that the distribution of mass error was near zero and most of them were less than 5 ppm (Fig. 2b), which means the mass accuracy of the MS data fits the requirement
Summary
Post-translational modifications (PTMs) play an important role in modulating diverse cellular processes, which can change protein functions by introducing new functional groups such as phospho, acetyl, ubiquityl and methyl groups (Huang et al 2015; Santos et al 2011). Utilization of microbial oils produced by oleaginous yeasts as sources in large-scale operations presents a great industrial interest. These microbial oils have been considered as one of the most suitable substitute for biodiesel production. In budding yeast Saccharomyces cerevisiae, 1059 acetylated proteins were identified, and a large proportion of acetylated proteins were implicated in the regulation of glycolysis/gluconeogenesis and amino acid metabolisms (Henriksen et al 2012). We wondered whether lysine acetylation plays an important role in the regulation of the production of lipid biosynthesis in oleaginous yeast
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