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Science 31 March 1989:
Vol. 243. no. 4899, pp. 1695 - 1699
DOI: 10.1126/science.2494702

Articles

Science, Vol 243, Issue 4899, 1695-1699
Copyright © 1989 by American Association for the Advancement of Science


articles

Parallel association of Fos and Jun leucine zippers juxtaposes DNA binding domains

R Gentz, FJ Rauscher 3rd, C Abate, and T Curran

Department of Molecular Oncology, Roche Institute of Molecular Biology, Nutley, NJ 07110.

The protein products of the fos and jun proto-oncogenes form a heterodimeric complex that participates in a stable high affinity interaction with DNA elements containing AP-1 binding sites. The effects of deletions and point mutations in Fos and Jun on protein complex formation and DNA binding have been examined. The data suggest that Fos and Jun dimerize via a parallel interaction of helical domains containing a heptad repeat of leucine residues (the leucine zipper). Dimerization is required for DNA binding and results in the appropriate juxtaposition of basic amino acid regions from Fos and Jun, both of which are required for association with DNA.


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