详细信息
Lysine Malonylome May Affect the Central Metabolism and Erythromycin Biosynthesis Pathway in Saccharopolyspora erythraea ( SCI-EXPANDED收录)
文献类型:期刊文献
英文题名:Lysine Malonylome May Affect the Central Metabolism and Erythromycin Biosynthesis Pathway in Saccharopolyspora erythraea
作者:Xu, Jun-Yu[1];Xu, Zhen[1];Zhou, Ying[1];Ye, Bang-Ce[1,2]
机构:[1]E China Univ Sci & Technol, State Key Lab Bioreactor Engn, Lab Biosyst & Microanal, Shanghai 200237, Peoples R China;[2]Shihezi Univ, Sch Chem & Chem Engn, Xinjiang 832000, Peoples R China
年份:2016
卷号:15
期号:5
起止页码:1685
外文期刊名:JOURNAL OF PROTEOME RESEARCH
收录:;WOS:【SCI-EXPANDED(收录号:WOS:000375891200027)】;
基金:This work was supported by grants from the China NSF (21276079 and 21335003) and SRFDP (20120074110009) of the Chinese Ministry of Education, the National Key Technologies R & D Programs (2014AA02150), and Fundamental Research Funds for the Central Universities.
语种:英文
外文关键词:protein acylation; malonylome; phosphorylome; Saccharopolyspora erythraea; post-translational modification; actinomycetes
摘要:Lysine acylation is a dynamic, reversible post-translational modification that can regulate cellular and organismal metabolism in bacteria. Acetylome has been studied well in bacteria. However, to our knowledge, there are no proteomic data on the lysine malonylation in prokaryotes, especially in actinomycetes, which are the major producers of therapeutic antibiotics. In our study, the first malonylome of the erythromycin-producing Saccharopolyspora erythraea was described by using a high-resolution mass spectrometry-based proteomics approach and high-affinity antimalonyllysine antibodies. We identified 192 malonylated sites on 132 substrates. Malonylated proteins are enriched in many biological processes such as protein synthesis, glycolysis and gluconeogenesis, the TCA cycle, and the feeder metabolic pathways of erythromycin synthesis according to GO analysis and KEGG pathway analysis. A total of 238 S/T/Y/H-phosphorylated sites on 158 proteins were also identified in our study, which aimed to explore the potential cross-talk between acylation and phosphorylation. After that, site-specific mutations showed that malonylation is a negative regulatory modification on the enzymatic activity of the acetyl-CoA synthetase (Acs) and glutamine synthetase (Gs). Furthermore, we compared the malonylation levels of the two-growth state to explore the potential effect of malonylation on the erythromycin biosynthesis. These findings expand our current knowledge of the actinomycetes malonylome and supplement the acylproteome databases of the whole bacteria.
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