T.D. Halazonetis, K. Georgopoulos, M.E. Greenberg, P. Leder, "c-Jun dimerizes with itself and with c-Fos, forming complexes of different DNA binding affinities," Cell, 55, 917-24, 2 December 1988.
Thanos Halazonetis (Harvard Medical School, Boston): "A number of cancer-causing genes (oncogenes) have been shown to code for factors regulating gene expression. The protein products of two such oncogenes, c-jun and c-fos, had been shown to be part of a protein complex that regulates the transcription of genes associated with cell division and differentiation. In this paper, we describe how the interaction of the Jun and Fos proteins modulates their DNA-binding activity. When the Jun and Fos proteins are cotranslated, they form a heterodimer of high specific DNA-binding activity. The two proteins have homologous domains that mediate heterodimer formation and subsequent DNA binding. The domain of the Jun protein, in addition to interacting with the homologous domain of the Fos protein, can ...
