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

Interaction of the Initiator Protein DnaA of Escherichia Coli With Its DNA Target

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Interaction of the Initiator Protein DnaA of Escherichia Coli With Its DNA Target

S Schaper et al. J Biol Chem. .
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Abstract

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.

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