Saccharopolyspora erythraea LC-MSMS

Lysine acetylation is a dynamic, reversible post-translational modification that is known to play an important role in regulating the activity of many key enzymes in bacteria. Acetylproteome studies have been performed on some bacteria. However, until now there have been no data on the Actinomycetes, which are the major producers of therapeutic antibiotics. In this study, we investigated the first acetylproteome of the erythromycin-producing Actinomycete Saccharopolyspora erythraea using a high-resolution mass spectrometry-based proteomics approach. Using immune-affinity isolation of acetyl-peptides with an anti-acetyllysine antibody followed by nano-UPLC/MS/MS analysis, we identified 664 unique lysine acetylated sites on 363 proteins.