Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli.
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Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y
Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli.
Mol Cell Proteomics. 2009 Feb;8(2):215-25. doi: 10.1074/mcp.M800187-MCP200. Epub 2008 Aug 23.
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- 18723842 [ View in PubMed]
- Abstract
Lysine acetylation and its regulatory enzymes are known to have pivotal roles in mammalian cellular physiology. However, the extent and function of this modification in prokaryotic cells remain largely unexplored, thereby presenting a hurdle to further functional study of this modification in prokaryotic systems. Here we report the first global screening of lysine acetylation, identifying 138 modification sites in 91 proteins from Escherichia coli. None of the proteins has been previously associated with this modification. Among the identified proteins are transcriptional regulators, as well as others with diverse functions. Interestingly, more than 70% of the acetylated proteins are metabolic enzymes and translation regulators, suggesting an intimate link of this modification to energy metabolism. The new dataset suggests that lysine acetylation could be abundant in prokaryotic cells. In addition, these results also imply that functions of lysine acetylation beyond regulation of gene expression are evolutionarily conserved from bacteria to mammals. Furthermore, we demonstrate that bacterial lysine acetylation is regulated in response to stress stimuli.
DrugBank Data that Cites this Article
- Polypeptides
Name UniProt ID DNA-directed RNA polymerase subunit beta P0A8V2 Details 30S ribosomal protein S12 P0A7S3 Details Adenylate kinase P69441 Details Isocitrate dehydrogenase [NADP] P08200 Details ADP-L-glycero-D-manno-heptose-6-epimerase P67910 Details Phosphoribosylglycinamide formyltransferase 2 P33221 Details Maltodextrin phosphorylase P00490 Details Formate acetyltransferase 1 P09373 Details Deoxyribose-phosphate aldolase P0A6L0 Details Pyruvate dehydrogenase E1 component P0AFG8 Details Phospho-2-dehydro-3-deoxyheptonate aldolase, Phe-sensitive P0AB91 Details Purine nucleoside phosphorylase DeoD-type P0ABP8 Details cAMP-activated global transcriptional regulator CRP P0ACJ8 Details Fructose-bisphosphate aldolase class 2 P0AB71 Details Tyrosine--tRNA ligase P0AGJ9 Details Glyceraldehyde-3-phosphate dehydrogenase A P0A9B2 Details Glutaminase 1 P77454 Details Alkyl hydroperoxide reductase subunit F P35340 Details Transketolase 1 P27302 Details Succinate dehydrogenase flavoprotein subunit P0AC41 Details DNA-directed RNA polymerase subunit beta' P0A8T7 Details Ribosome-recycling factor P0A805 Details