The diversity of lysine-acetylated proteins in Escherichia coli.

摘要: Acetylation of lysine residues in proteins is a reversible and highly regulated posttranslational modification. However, it has not been systematically studied prokaryotes. By affinity immunoseparation using an anti-acetyllysine antibody together with nano-HPLC/MS/MS, we identified 125 lysineacetylated sites 85 among derived from Escherichia coli. The lysine-acetylated are involved diverse cellular functions including protein synthesis, carbohydrate metabolism, the TCA cycle, nucleotide amino acid chaperones, transcription. Interestingly, found higher level acetylation during stationary phase than exponential phase; acetylated were immediately deacetylated when cells transferred to fresh LB culture medium. These results demonstrate that abundant E. coli might be modifying or regulating activities various enzymes critical metabolic processes synthesis building blocks response environmental changes.