YcgC represents a new protein deacetylase family in prokaryotes

Shun Tu, Shu Juan Guo, Chien Sheng Chen, Cheng Xi Liu, He Wei Jiang, Feng Ge, Jiao Yu Deng, Yi Ming Zhou, Daniel M. Czajkowsky, Yang Li, Bang Ruo Qi, Young Hoon Ahn, Philip A. Cole, Heng Zhu, Sheng Ce Tao

Research output: Contribution to journalArticlepeer-review


Reversible lysine acetylation is one of the most important protein posttranslational modifications that plays essential roles in both prokaryotes and eukaryotes. However, only a few lysine deacetylases (KDACs) have been identified in prokaryotes, perhaps in part due to their limited sequence homology. Herein, we developed a ‘clip-chip’ strategy to enable unbiased, activity-based discovery of novel KDACs in the Escherichia coli proteome. In-depth biochemical characterization confirmed that YcgC is a serine hydrolase involving Ser200 as the catalytic nucleophile for lysine deacetylation and does not use NAD+ or Zn2+ like other established KDACs. Further, in vivo characterization demonstrated that YcgC regulates transcription by catalyzing deacetylation of Lys52 and Lys62 of a transcriptional repressor RutR. Importantly, YcgC targets a distinct set of substrates from the only known E. coli KDAC CobB. Analysis of YcgC’s bacterial homologs confirmed that they also exhibit KDAC activity. YcgC thus represents a novel family of prokaryotic KDACs.

Original languageEnglish (US)
Article numbere05322
Issue numberDECEMBER2015
StatePublished - Dec 30 2015

ASJC Scopus subject areas

  • Neuroscience(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)


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