Interaction of the initiator protein DnaA of Escherichia coli with its DNA target

J Biol Chem. 1995 Jul 21;270(29):17622-6. doi: 10.1074/jbc.270.29.17622.


Equilibrium and kinetic rate constants were determined for the binding of the initiator protein DnaA of Escherichia coli to its binding site, the non-palindromic 9-bp DnaA box, using gel retardation techniques. The dissociation constant for specific binding was between 1 and 50 nM for individual DnaA boxes on 21-bp double-stranded oligonucleotides. Only DnaA boxes of the sequence TT(A/T)TNCACA resulted in specific fragment retention. Both the 9-bp consensus sequence and flanking sequences determined the binding efficiency. One DnaA monomer was found to bind to a DnaA box and to induce a bend of about 40 degrees.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / metabolism*
  • Base Sequence
  • Binding Sites
  • DNA / metabolism*
  • DNA Replication*
  • DNA-Binding Proteins / metabolism*
  • Escherichia coli / genetics*
  • Kinetics
  • Molecular Sequence Data


  • Bacterial Proteins
  • DNA-Binding Proteins
  • DnaA protein, Bacteria
  • DNA