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PubMed · 2518685

fos-jun Conspiracy: implications for the cell.

I M Verma·L J Ransone·J Visvader·P Sassone-Corsi·W W Lamph
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Abstract

Two nuclear oncoproteins, fos and jun (AP-1), cooperate in forming a very stable heterodimeric complex that binds to the AP-1 site with increased affinity. The 'leucine zipper' domain of both fos and jun is necessary for the formation of this heterodimer. Mutations of single residues within the leucine zipper domain had no effect on protein complex formation. However, mutagenesis of the first leucine of the heptad repeat in either fos or jun basic regions and alteration of the spacing between the basic and leucine zipper domains indicate that the basic region of fos has a crucial role in determining the DNA binding affinity of the transcriptional complex. Mutations of the basic amino acids in fos protein prevent binding to TPA (phorbol ester)-responsive element (TRE) in the presence of wild-type jun protein. Thus fos protein appears to be dominant in jun-fos binding to DNA, even though fos alone cannot bind to TRE. Mutants in the basic regions of fos and jun can be exploited as dominant-negative mutants to ablate their normal cellular function.

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Amino Acid SequenceAnimalsCell Transformation, NeoplasticDNADNA-Binding ProteinsGene Expression RegulationLeucine ZippersMiceMolecular Sequence DataOncogenesProtein BindingProtein ConformationProto-Oncogene ProteinsProto-Oncogene Proteins c-fosProto-Oncogene Proteins c-junProto-OncogenesSignal TransductionTranscription FactorsJournal ArticleResearch Support, Non-U.S. Gov'tResearch Support, U.S. Gov't, P.H.S.Review

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I M Verma, L J Ransone, J Visvader, P Sassone-Corsi, W W Lamph. 1989. fos-jun Conspiracy: implications for the cell.. https://pubmed.ncbi.nlm.nih.gov/2518685/

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