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Dimer formation by ternary complex factor ELK-1.

V Drewett·S Muller·J Goodall·P E Shaw
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Abstract

Ternary complex factors (TCFs), a subgroup of the ets protein family, bind with a dimer of serum response factor to the c-fos serum response element. Both DNA binding and transcriptional activation by TCFs are regulated by mitogen-activated protein kinases. When activated, mitogen-activated protein kinases form homodimers that translocate to the nucleus, where they interact with TCFs via specific docking sites. Here we show by three different criteria that Elk-1 is capable of forming dimers in eukaryotic cells through two distinct interaction domains. These observations are consistent with a dynamic model of TCF-promoter interactions.

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AnimalsBlotting, WesternCOS CellsCell LineChromatography, GelDNA-Binding ProteinsDimerizationGene DeletionGene Expression RegulationHumansModels, GeneticMutagenesisPlasmidsPromoter Regions, GeneticProto-Oncogene ProteinsTranscription FactorsTransfectionets-Domain Protein Elk-1ets-Domain Protein Elk-4Journal ArticleResearch Support, Non-U.S. Gov't

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V Drewett, S Muller, J Goodall, P E Shaw. 2000-01-21. Dimer formation by ternary complex factor ELK-1.. https://doi.org/10.1074/jbc.275.3.1757

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