Abstract
As a novel protein post-translational modification, lysine succinylation is widely involved in metabolism regulation. To describe succinylated lysine's physiological functions and distribution patterns in Saccharopolyspora erythraea, a large and global protein succinylome was identified in a hypersuccinylated strain E3ΔsucC, using high-resolution 4D label-free mass spectrometry. Bioinformatic analysis was conducted to examine the succinylated proteins further in this study. The results showed that succinylated proteins were identified to be predominantly involved in protein synthesis, central carbon and nitrogen metabolism, and secondary metabolism. The process of lysine succinylation was found intricately regulated by a delicate interplay of factors, such as the relative abundance of lysine within the protein, the strategic positioning of polar amino acids flanking the succinylated sites, and the degree to which lysine residues are exposed to the solvent, thereby shaping the landscape of post-translational modifications. This systematic analysis represents the global analysis of lysine succinylation in S. erythraea and provides an important resource for exploring the the function of Ksucc and regulation in S. erythraea and likely in all actinomycetes.