Appl Microbiol Biotechnology: the first discovery of lysine acetylation profile of Actinomycetes

In February 2015, researchers from ye bangce Laboratory of East China University of science and technology and Hangzhou Jingjie Biotechnology Co., Ltd published the latest research progress in post-translational modification of actinomycete protein in appl Microbiol biotechnology, and published the first lysine acetylation modification spectrum of actinomycete Lysine acetylation is a dynamic and reversible post-translational modification, which is widely known in the bacteria to regulate the activity of core enzymes It plays an important role in the transcription, translation and metabolism of bacteria At present, acetylated proteome analysis has been found in E.coli, Salmonella, Bacillus subtilis, Bacillus thermophilus, Erwinia and thermophilic bacteria The results show that L-lysine acetylation is widely present in bacterial proteins and participates in protein synthesis, metabolism, stress response and detoxification metabolism However, there is no data on the acetylation group of actinomycetes, the antibiotic manufacturers needed for treatment Using proteomic methods based on high-resolution mass spectrometry, the researchers first analyzed the acetylation groups in erythromycin, the producer of erythromycin Firstly, the acetylated peptide was enriched by the acetylated pan antibody (PTM biolab, Inc.) and then analyzed by liquid chromatography tandem mass spectrometry A total of 664 L-lysine acetylation sites were identified on 363 proteins These acetylated proteins are involved in many biological processes, such as protein synthesis, glycolysis or gluconeogenesis, citric acid (TCA) cycle, fatty acid metabolism, secondary metabolism and erythromycin synthesis According to go and KEGG pathways, the researchers analyzed the cell functions of the acetylated group data, and found that there were four pattern sequences around the acetylated site: KACh, kacxxxxk, kacxxxxrand kacy These results show that acetylation is widely existed in actinomycetes, which extends our knowledge of bacterial acetylation proteome, and provides clues for the regulation of acetylation in primary and secondary metabolism The researchers identified two acetylated enzymes directly related to the secondary metabolism in erythromyces saccharopolysporus: (1) tdp-4-one-6-deoxyhexose 2,3-reductase, which is related to the biosynthesis of erythromycin; (2) non ribosomal peptide synthetase, which is related to the biosynthesis of iron-containing cells The discovery of these two enzymes indicates that acetylation modification has a direct regulatory effect on the synthesis of antibiotics in actinomycetes Actinomycetes are often used to overproduce antibiotics by gene modification, which usually increases the activity of specific regulatory proteins and / or over expressed core enzymes in precursor pathway and biosynthesis pathway However, these genetically engineered strains did not make full use of the overall regulatory mechanism of the reversible acylation of lysine Therefore, a more thorough study and optimization of lysine acylation of secondary metabolic enzymes can provide a new way for efficient production of industrial strains Article source: lysine acylproterme analysis suggestions its roles in primary and secondary metabolism in Saccharopolyspora eritraea