Reversible lysine acetylation is involved in DNA replication initiation by regulating activities of initiator DnaA in Escherichia coli

Sci Rep. 2016 Aug 3:6:30837. doi: 10.1038/srep30837.

Abstract

The regulation of chromosomal replication is critical and the activation of DnaA by ATP binding is a key step in replication initiation. However, it remains unclear whether and how the process of ATP-binding to DnaA is regulated. Here, we show that DnaA can be acetylated, and its acetylation level varies with cell growth and correlates with DNA replication initiation frequencies in E. coli. Specifically, the conserved K178 in Walker A motif of DnaA can be acetylated and its acetylation level reaches the summit at the stationary phase, which prevents DnaA from binding to ATP or oriC and leads to inhibition of DNA replication initiation. The deacetylation process of DnaA is catalyzed by deacetylase CobB. The acetylation process of DnaA is mediated by acetyltransferase YfiQ, and nonenzymatically by acetyl-phosphate. These findings suggest that the reversible acetylation of DnaA ensures cells to respond promptly to environmental changes. Since Walker A motif is universally distributed across organisms, acetylation of Walker A motif may present a novel regulatory mechanism conserved from bacteria to eukaryotes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylation
  • Adenosine Triphosphate / metabolism
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • DNA Replication*
  • DNA, Bacterial / genetics
  • DNA-Binding Proteins / genetics
  • DNA-Binding Proteins / metabolism*
  • Escherichia coli / genetics*
  • Escherichia coli / metabolism
  • Escherichia coli Proteins / genetics
  • Escherichia coli Proteins / metabolism*
  • Lysine / chemistry*
  • Lysine / metabolism
  • Organophosphates / metabolism*
  • Phosphotransferases / genetics
  • Phosphotransferases / metabolism*
  • Replication Origin*

Substances

  • Bacterial Proteins
  • DNA, Bacterial
  • DNA-Binding Proteins
  • DnaA protein, Bacteria
  • Escherichia coli Proteins
  • Organophosphates
  • acetyl phosphate
  • Adenosine Triphosphate
  • Phosphotransferases
  • NadK protein, E coli
  • Lysine