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Science 1 March 1991:
Vol. 251. no. 4997, pp. 1067 - 1071
DOI: 10.1126/science.1998122
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Articles

Science, Vol 251, Issue 4997, 1067-1071
Copyright © 1991 by American Association for the Advancement of Science

articles

Characterization of a dimerization motif in AP-2 and its function in heterologous DNA-binding proteins

T Williams and R Tjian

Howard Hughes Medical Institute, Department of Molecular and Cell Biology, University of California, Berkeley 94720.

The mammalian transcription factor AP-2 is a retinoic acid inducible sequence-specific DNA-binding protein that is developmentally regulated. In this report, the functional domains necessary for AP-2 DNA binding were studied. AP-2 required a dimerization domain and an adjacent region of net basic charge to achieve a sequence-specific protein:DNA interaction. The sequences responsible for dimerization consisted of two putative amphipathic alpha helices separated by a large intervening span region. This helix-span-helix (HSH) domain was unable to bind DNA when separated from the basic region, but was still capable of dimerization. The ability of the HSH domain to function as a module that promotes DNA binding through dimerization was further demonstrated by attaching it to the heterologous basic region of the c-Jun proto-oncogene product. The resulting chimeric protein specifically recognized an AP-1 DNA-binding site in the absence of an intact c-Jun leucine repeat and in a manner that was dependent on the presence of a functional AP-2 dimerization domain.


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