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Nucleic Acids Research, 1975, Vol. 2, No. 10 1821-1838
© 1975

Articles

Physical studies of the interaction between the Escherichia coli DNA binding protein and nucleic acids

Ian J. Molineux+, Andrew Pauli and Malcolm L. Gefter

Department of Biology, Massachusetts Institute of Technology Cambridge, MA 02139, USA

Received August 18, 1975.

The interaction of nucleic acid with the Escherichia coli DNA-binding protein has been studied by fluorescence emission spectroscopy and sedimentation velocity analysis. The protein binds to single-strand DNA with an apparent equilibrium dissociation constant of 2 x 10–9. It binds to the homopolymers poly(dA) and poly(dT) slightly more tightly, but has a larger apparent equilibrium dissociation constant to poly(dC). The protein also binds tightly to ribohomopolymers and to tRNA, but not to duplex DNA. By the use of defined-length oligonucleotides, it has been shown that the protein binds to DNA in a highly cooperative manner. The extent of cooperativity is seen as the difference in binding between an isolated monomeric protein molecule bound to DNA and two or more molecules binding to contiguous sites.

+ Present address: Imperial Cancer Research Fund, Burtonhole Road, London NW7 1AD, England


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