Proteome-wide Lysine Glutarylation Profiling of the Mycobacterium tuberculosis H37Rv
2016
Xie, Longxiang | Wang, Guirong | Yu, Zhaoxiao | Zhou, Mingliang | Li, Qiming | Huang, Hairong | Xie, Jianping
Lysine glutarylation, a new protein posttranslational modification (PTM), was recently identified and characterized in both prokaryotic and eukaryotic cells. To explore the distribution of lysine glutarylation in Mycobacterium tuberculsosis, by using a comprehensive method combining the immune affinity peptide enrichment by the glutaryl-lysine antibody with LC–MS, we finally identified 41 glutarylation sites in 24 glutarylated proteins from M. tuberculosis. These glutarylated proteins are involved in various cellular functions such as translation and metabolism and exhibit diverse subcellular localizations. Three common glutarylated proteins including 50S ribosomal protein L7/L12, elongation factor Tu, and dihydrolipoamide succinyltransferase are shared between Escherichia coli and M. tuberculosis. Moreover, comparison with other PTMs characterized in M. tuberculosis, 15 glutarylated proteins, are found to be both acetylated and succinylated. Notably, several stress-response-associated proteins including HspX are glutarylated. Our data provide the first analysis of M. tuberculosis lysine glutarylated proteins. Further studies on the role of the glutarylated proteins will unveil the molecular mechanisms of glutarylation underlying M. tuberculosis physiology and pathogenesis.
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