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J. Biol. Chem., Vol. 266, Issue 1, 252-260, 01, 1991
U Zabel, R Schreck and PA Baeuerle
A rapid purification procedure for the NF-kappa B transcription factor from
the cytosol of human placenta is demonstrated which exploits the
insensitivity of the NF-kappa B.DNA complex toward the intercalating agent
chloroquine. Purified NF-kappa B required 100 mM KCl or NaCl and a pH of
7.5 to optimally bind to DNA. Equilibrium of binding was reached within
less than 5 min in the absence of competitor DNA and after 1 h in the
presence of 0.1 mg/ml poly(dI-dC). DNA binding of NF- kappa B was
specifically blocked by the chelating agent 1,10- orthophenantroline and
could only be reconstituted by addition of Zn2+. Under optimal binding
conditions, the dissociation constant for the complex of the purified
NF-kappa B with its most frequent cognate DNA motif 5'-GGGACTTTCC-3' was in
the range of 10(-12) to 10(-13) M. Various other cis-acting kappa B motifs
were recognized by NF-kappa B with lower affinities. A comparative analysis
of known NF-kappa B- binding sites and competition experiments with
synthetic polynucleotides and oligonucleotides encompassing only one
half-site or single-stranded kappa B motifs suggested that the two
DNA-binding monomers in the NF-kappa B protein complex can interact
differentially with the half-sites of the decameric cognate motif.
DNA binding of purified transcription factor NF-kappa B. Affinity, specificity, Zn2+ dependence, and differential half-site recognition
Laboratory for Molecular Biology, Ludwig-Maximilians-University Munich, Martinsried, Federal Republic of Germany.
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