Revealing the lysine acetylation modification spectrum of actinomycetes for the first time
Revealing the lysine acetylation modification spectrum of actinomycetes for the first time
May 08, 2015 Source: Bio Valley
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In February 2015, researchers from East China University of Science and Technology Ye Bangce Laboratory and Hangzhou Jingjie Biotechnology Co., Ltd. published the latest research progress on post-translational modification of actinomycetes in Appl Microbiol Biotechnol. Lysine acetylation modification spectrum.
Lysine acetylation is a dynamic, reversible post-translational modification known to be ubiquitous in bacteria to regulate core enzyme activity, playing an important role in bacterial transcription, translation and metabolism. Acetylation proteome analysis has been performed in various microorganisms such as Escherichia coli, Salmonella, Bacillus subtilis, Bacillus thermophilus, Erwinia and thermophilic bacteria, and the results indicate that lysine acetylation is widely present in bacterial proteins. And involved in protein synthesis, metabolism, stress response and detoxification metabolism. However, there has been no data on the acetylation group of actinomycetes, the antibiotic manufacturer used for the treatment.
The researchers used a proteomic approach based on high-resolution mass spectrometry to first analyze the acetylation group in the genus Rhodosporidium erythropolis (the producer of erythromycin). First, the acetylated modified peptide was immunoaffinity-enriched by acetylated pan-antibody (PTM Biolab, Inc.), and then 665 lysine acetylation sites were identified by liquid chromatography-tandem mass spectrometry. 363 proteins. These acetylated proteins are involved in a variety of biological processes such as protein synthesis, glycolysis or gluconeogenesis, citric acid (TCA) cycling, fatty acid metabolism, secondary metabolism, and metabolic pathways for erythromycin synthesis.
The researchers then performed different cell function analyses on the obtained acetylation group data based on GO and KEGG pathways, and found that there are four pattern sequences around the acetylation site, KACH, KACXXXXK, KACXXXXR, KACY. These results indicate that acetylation is widely present in actinomycetes, extending our current knowledge of bacterial acetylated proteomes and providing clues to the regulatory functions of acetylation in primary and secondary metabolism.
The researchers identified two enzymes that are directly involved in secondary metabolism, such as TDP-4-keto-6-deoxyhexose 2,3-reductase, in the S. erythraea. Related to the biosynthesis of erythromycin; (2) non-ribosomal peptide synthetase, associated with the biosynthesis of iron-containing cells. The discovery of these two enzymes indicates that the acetylation modification has a direct regulatory effect on the synthesis of antibiotics in actinomycetes.
Actinomycetes are often genetically engineered to overproduce antibiotics, and the engineering of such strains typically increases the activity of specific regulatory proteins and/or overexpressing core enzymes in the precursor pathway and biosynthetic pathway. However, these genetically engineered strains do not fully utilize the overall regulatory mechanisms of reversible acylation of lysine. Therefore, a more thorough research and optimization of lysine acylation modifications involved in secondary metabolic enzymes can provide a new way for efficient production of industrial strains.
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