Integrated Succinylome and Metabolome Profiling Reveals Crucial Role of S-Ribosylhomocysteine Lyase in Quorum Sensing and Metabolism of .

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ID: 67466
2019
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Abstract
Protein modification by lysine succinylation is a newly identified post-translational modification (PTM) of lysine residues and plays an important role in diverse physiological functions, although their associated biological characteristics are still largely unknown. Here, we investigated the effects of lysine succinylation on the physiological regulation within a well-known fish pathogen, A high affinity purification method was used to enrich peptides with lysine succinylation in ATCC 7966, and a total of 2,174 lysine succinylation sites were identified on 666 proteins using LC-MS/MS. Gene ontology analysis indicated that these succinylated proteins are involved in diverse metabolic pathways and biological processes, including translation, protein export, and central metabolic pathways. The modifications of several selected candidates were further validated by Western blotting. Using site-directed mutagenesis, we observed that the succinylation of lysines on S-ribosylhomocysteine lyase (LuxS) at the K23 and K30 sites positively regulate the production of the quorum sensing autoinducer AI-2, and that these PTMs ultimately alter its competitiveness with another pathogen, Moreover, subsequent metabolomic analyses indicated that K30 succinylation on LuxS may suppress the activated methyl cycle (AMC) and that both the K23 and K30 sites are involved in amino acid metabolism. Taken together, the results from this study provide significant insights into the functions of lysine succinylation and its critical roles on LuxS in regulating the cellular physiology of
Reference Key
yao2019integratedmolecular Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Yao, Zujie;Guo, Zhuang;Wang, Yuqian;Li, Wanxin;Fu, Yuying;Lin, Yuexu;Lin, Wenxiong;Lin, Xiangmin;
Journal molecular & cellular proteomics : mcp
Year 2019
DOI
10.1074/mcp.RA118.001035
URL
Keywords
Microbiology Mass spectrometry metabolomics quorum sensing post-translational modifications activated methyl cycle affinity proteomics s-ribosylhomocysteine lyase succinylome

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