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Oncogene. 1991 Apr;6(4):533-42.

c-JUN, JUN B, and JUN D differ in their binding affinities to AP-1 and CRE consensus sequences: effect of FOS proteins.

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Bristol-Myers Squibb Pharmaceutical Research Institute, Department of Molecular Biology, Princeton, New Jersey 08543-4000.


We have compared the binding properties of c-JUN, JUN B, and JUN D in the absence or in the presence of c-FOS, FOS B, and FRA-1 to different AP-1 and CRE-containing oligonucleotides. The results demonstrate that for a given AP-1-containing oligonucleotide the binding affinities of the different JUN proteins are always c-JUN greater than JUN D greater than JUN B. The three JUN proteins have the capacity to bind to a CRE consensus sequence with very high affinity. We have found that c-JUN, JUN B, and JUN D bind with different affinities to different oligonucleotides containing an identical AP-1 or CRE binding site, implying that the adjacent sequences influence the stability of the JUN/DNA complexes. Interestingly, an AP-1-containing oligonucleotide which binds the JUN proteins with high affinity can be converted to a CRE-containing oligonucleotide which will also bind the different JUNs very efficiently. The heterodimers formed between the different JUN and FOS proteins have an enhanced binding activity compared to the JUN:JUN homodimers. In all cases the half-lives of the JUN:FOS/DNA complexes are longer than those of the JUN:JUN/DNA complexes. The most stable complexes were obtained in the presence of FOS B, followed by FRA-1 and c-FOS.

[Indexed for MEDLINE]

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