ATP- and ADP-dnaA protein, a molecular switch in gene regulation

EMBO J. 1999 Nov 1;18(21):6169-76. doi: 10.1093/emboj/18.21.6169.


DnaA protein functions by binding to asymmetric 9mer DNA sites, the DnaA boxes. ATP-DnaA and ADP-DnaA bind to 9mer DnaA boxes with equal affinity, but only ATP-DnaA protein binds in addition to an as yet unknown 6mer site, the ATP-DnaA box AGATCT, or a close match to it. ATP-DnaA protein binding to ATP-DnaA boxes is restricted to sites located in close proximity to DnaA boxes, suggesting that protein-protein interaction is required for its stabilization. We show that ATP-DnaA represses dnaA transcription much more efficiently than ADP-DnaA. DnaA is thus a regulatory molecule that, depending on the adenosine nucleotide bound, can bind to different sequences and thereby fulfill distinct functions.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Diphosphate / metabolism*
  • Adenosine Triphosphate / metabolism*
  • Bacterial Proteins / genetics*
  • Base Sequence
  • Binding Sites
  • Cell Cycle / genetics
  • DNA / metabolism*
  • DNA Footprinting
  • DNA Replication / genetics
  • DNA-Binding Proteins / genetics*
  • Escherichia coli / genetics
  • Gene Expression Regulation
  • Kinetics
  • Molecular Sequence Data
  • Oligodeoxyribonucleotides / metabolism
  • Promoter Regions, Genetic
  • Repressor Proteins / pharmacology
  • Transcription, Genetic


  • Bacterial Proteins
  • DNA-Binding Proteins
  • DnaA protein, Bacteria
  • Oligodeoxyribonucleotides
  • Repressor Proteins
  • Adenosine Diphosphate
  • Adenosine Triphosphate
  • DNA