文献类型：期刊文献

英文题名：Lysine acetylproteome analysis suggests its roles in primary and secondary metabolism in Saccharopolyspora erythraea

作者：Huang, Dan[1];Li, Zhi-Hai[1];You, Di[1];Zhou, Ying[1];Ye, Bang-Ce[1]

机构：[1]E China Univ Sci & Technol, Lab Biosyst & Microanal, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China

年份：2015

卷号：99

期号：3

起止页码：1399

外文期刊名：APPLIED MICROBIOLOGY AND BIOTECHNOLOGY

收录：;EI(收录号：20145100331430);WOS:【SCI-EXPANDED(收录号:WOS:000348771400032)】；

基金：This work was financially supported by grants from the National Key Technologies R&D Program (2014AA021502), the National Natural Science Foundation of China (21276079, 31401592) and SRFDP (No. 20120074110009). We thank Prof. Yingming Zhao at University of Chicago for critical reading of the manuscript and helpful comments.

语种：英文

外文关键词：Protein acetylation; Acetylome; Saccharopolyspora erythraea; Posttranslational modification; Actinomycetes

摘要：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 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 ultra performance liquid chromatography tandem mass spectroscopy (nanoUPLC-MS/MS) analysis, we identified 664 unique lysine-acetylated sites on 363 proteins. Acetylated proteins are involved in many biological processes such as protein synthesis, glycolysis/gluconeogenesis, citric acid (TCA) cycle, fatty acid metabolism, secondary metabolism, and the feeder metabolic pathways of erythromycin synthesis. We characterized the acetylproteome and analyzed in detail the impact of acetylation on diverse cellular functions according to Gene Ontology and Kyoto Encyclopedia of Genes and Genomes (KEGG) pathways. Four motif sequences surrounding the acetylation sites ((KH)-H-AC, (KY)-Y-AC, (KXXXXR)-X-AC, and (KXXXXK)-X-AC) were found in the S. erythraea acetylproteome. These findings suggest that abundant lysine acetylation occurs in Actinomycetes, expand our current knowledge of the bacterial acetylproteome, and provide insight into the regulatory function of acetylation in primary and secondary metabolism.