A Fos protein containing the Jun leucine zipper forms a homodimer which binds to the AP1 binding site

Nature
M NeubergR Müller

Abstract

The TPA (12-O-tetradecanoyl-phorbol-13-acetate) responsive element (TRE) is recognized by the inducible transcription factor AP1, a heterodimeric complex of Fos- and Jun-protein subunits, which each contain a specific structure known as the leucine zipper through which they interact. Studies using site-directed mutagenesis have shown that a basic region adjacent to the leucine zipper in Fos is crucial for the interaction of the Fos-Jun complex with the TRE, and probably represents a site of interaction with DNA. The functionally crucial amino acids in this region are almost completely conserved between Fos and Jun (refs 6, 7 and 11; M.N. and R.M., unpublished results), indicating the formation of a nearly symmetrical DNA-binding site in the Fos-Jun complex. Whereas Jun can form a homodimeric protein complex which binds to the TRE, Fos is unable to do so. The Fos-Jun heterodimer, however, possesses at least a 30-fold-higher affinity for the TRE than does the Jun-Jun homodimer, indicating cooperative binding. Because Fos cannot form a homodimer it is not known whether Fos specifically recognizes part of the TRE or has a different role in the binding of the Fos-Jun complex to DNA. Here we report that exchanging the leucine zipper ...Continue Reading

References

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