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.

PubMed ID
18723842 [ View in PubMed
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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
NameUniProt ID
DNA-directed RNA polymerase subunit betaP0A8V2Details
30S ribosomal protein S12P0A7S3Details
Adenylate kinaseP69441Details
Isocitrate dehydrogenase [NADP]P08200Details
ADP-L-glycero-D-manno-heptose-6-epimeraseP67910Details
Phosphoribosylglycinamide formyltransferase 2P33221Details
Maltodextrin phosphorylaseP00490Details
Formate acetyltransferase 1P09373Details
Deoxyribose-phosphate aldolaseP0A6L0Details
Pyruvate dehydrogenase E1 componentP0AFG8Details
Phospho-2-dehydro-3-deoxyheptonate aldolase, Phe-sensitiveP0AB91Details
Purine nucleoside phosphorylase DeoD-typeP0ABP8Details
cAMP-activated global transcriptional regulator CRPP0ACJ8Details
Fructose-bisphosphate aldolase class 2P0AB71Details
Tyrosine--tRNA ligaseP0AGJ9Details
Glyceraldehyde-3-phosphate dehydrogenase AP0A9B2Details
Glutaminase 1P77454Details
Alkyl hydroperoxide reductase subunit FP35340Details
Transketolase 1P27302Details
Succinate dehydrogenase flavoprotein subunitP0AC41Details
DNA-directed RNA polymerase subunit beta'P0A8T7Details
Ribosome-recycling factorP0A805Details