PMID: 2113670Jun 1, 1990Paper

Analysis of dimerization and DNA binding functions in Fos and Jun by domain-swapping: involvement of residues outside the leucine zipper/basic region

Oncogene
D R Cohen, T Curran

Abstract

The products of two cellular proto-oncogenes c-fos and c-jun form a heterodimeric complex that contribute to the DNA-binding activity referred to as AP-1 (activator protein-1). Two domains have been proposed to be required for heterodimer formation and protein-DNA complex formation. The leucine zipper domain mediated the interaction between the two proteins and a highly basic region immediately N-terminal to the leucine zipper forms a DNA binding domain. To assess the role of these two domains in dimerization and DNA binding and to determine what contribution, if any, is made by residues outside of these regions, we carried out an extensive domain swap analysis. Restriction sites created in the fos and jun cDNAs flanking the basic region and leucine zipper allowed these domains to be swapped between the two proteins either singly or in various combinations with adjacent domains. The chimeric proteins were assayed for their ability to dimerize with each other and to interact with the AP-1 consensus sequence. It was found that two Jun leucine zipper regions could mediate protein dimerization, whereas two Fos leucine zipper regions could not. The dimers formed between two Jun leucine repeats were less stable than those formed betw...Continue Reading

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