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Nucleic Acids Research, 1979, Vol. 6, No. 6 2217-2236
© 1979

Articles

Equilibrium and kinetic aspects of protein-DNA recognition

M.A. Livhitz, G.V. Gursky, A.S. Zasedatelev and M.V. Volkenstein

Institute of Molecular Biology, USSR Academy of Sciences Moscow 117984, USSR

Received March 12, 1979. The specificity of regulatory protein binding to DNA is due to a complementarity between the sequence of reaction centres on the protein and the base pair sequence in the specific DNA site allowing the formation of a number of specific noncovalent bonds between the interacting entities. In the present communication the thermodynamic and kinetic aspects of these interactions are considered. The extent of binding specificity is shown to increase with an increase of the bond stability constants and with an increase in the number of ligand reaction centres. Kinetic analysis is carried out assuming that association process is very fast and that dissociation of nonspecific complexes is a ratelimiting step in the recognition of a specific binding site on DNA. The calculations show that a ligand can recognize its specific binding site on DNA within a reasonably limited time interval if the number of its reaction centres and the correspon ding stability constants are strongly limited.


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