Acetyl Phosphate Acetylates Proteins of Streptomyces coelicolor M-145

Abstract

Abstract: Protein Nε-lysine acetylation is a ubiquitous posttranslational modification. Acetylation in eukaryotes and prokaryotes can perform by acetylases or nonenzymatically using acetyl phosphate. Proteins involved in the carbon metabolism of Streptomyces coelicolor M-145 have been determined to be acetylated. Here, acetylation by acetyl phosphate of purified recombinant isocitrate dehydrogenase, malate dehydrogenase, phosphoenolpyruvate carboxylase, and phosphoenolpyruvate carboxykinase from S. coelicolor is reported. The enzymatic activities of isocitrate and malate dehydrogenases were negatively affected by acetylation, suggesting that acetyl phosphate could act as a metabolic regulator of glucose assimilation in this microorganism. To our knowledge, this is the first time that protein acetylation by acetyl phosphate has been reported in a streptomycete.