Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli

Junmei Zhang, Robert Sprung, Jimin Pei, Xiaohong Tan, Sungchan Kim, Heng Zhu, Chuan Fa Liu, Nick V. Grishin, Ying Zhao

Research output: Contribution to journalArticlepeer-review

395 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)215-225
Number of pages11
JournalMolecular and Cellular Proteomics
Issue number2
StatePublished - Feb 2009

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry
  • Molecular Biology


Dive into the research topics of 'Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli'. Together they form a unique fingerprint.

Cite this